{"gene":"TG_261950","gene_symbol":"ATPB","run_date":"2026-09-10T21:09:19","timeline":{"discoveries":[{"year":2018,"finding":"The F-type ATP synthase complex of T. gondii, which includes the canonical beta subunit (ATPB), was partially purified in monomeric (~600 kDa) and dimeric (>1 MDa) forms; mass spectrometry identified 20 novel subunits alongside core subunits, and key FO subunits a, b, and d were identified from conserved structural features despite extreme sequence diversification.","method":"Partial purification of native complex followed by mass spectrometry; bioinformatic identification of conserved structural features","journal":"PLoS biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — native complex purification with MS identification, single lab, two orthogonal methods (biochemical fractionation + MS)","pmids":["30005062"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"The apicomplexan F-type ATP synthase complex, which includes ATPB, assembles into cyclic hexamers that shape the distinct tubular cristae morphology of T. gondii mitochondria; cryo-EM structure of the hexamer revealed 17 apicomplexan-specific subunits, an extensive dimer interface including bound cardiolipins and inhibitor IF1, and cryo-ET showed hexamers arrange into ~20-MDa pentagonal pyramids at curved apical membrane regions; knockout of linker subunit ATPTG11 disrupted pentagonal pyramids and caused aberrant cristae morphology.","method":"Cryo-EM structure determination; cryo-ET with subtomogram averaging; genetic knockout with phenotypic analysis of cristae morphology","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-EM structure plus cryo-ET plus functional genetic knockout, multiple orthogonal methods in one rigorous study","pmids":["33402698"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Complexome profiling of T. gondii mitochondria using a proteomic approach assigned 60 proteins to complexes II, IV, and the F1Fo-ATP synthase (which includes ATPB), identifying 16 previously uncharacterized subunits and establishing the divergent subunit composition of the apicomplexan F1Fo-ATP synthase.","method":"Complexome profiling (blue-native PAGE coupled with quantitative mass spectrometry)","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — complexome profiling with quantitative MS, single lab, systematic biochemical approach","pmids":["33651838"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"ATPB is the beta subunit of the mitochondrial F-type ATP synthase in Toxoplasma gondii; the complex assembles into cyclic hexamers that form ~20-MDa pentagonal pyramidal arrays at curved apical inner membrane regions, shaping the parasite's distinctive tubular cristae, with the hexamer structure determined by cryo-EM revealing 17 apicomplexan-specific accessory subunits alongside core subunits including cardiolipin and inhibitor IF1 at the dimer interface."},"narrative":{"mechanistic_narrative":"ATPB is the beta subunit of the divergent mitochondrial F-type (F1Fo) ATP synthase of Toxoplasma gondii, a complex whose organization shapes the parasite's characteristic tubular cristae [PMID:30005062, PMID:33402698]. The complex was purified as monomeric (~600 kDa) and dimeric (>1 MDa) native forms, and mass spectrometry, complexome profiling, and cryo-EM together established a highly divergent subunit composition, with core subunits accompanied by roughly 17 apicomplexan-specific accessory subunits, extensively diversified FO subunits a, b, and d, and bound cardiolipins and the inhibitor IF1 at the dimer interface [PMID:30005062, PMID:33402698, PMID:33651838]. Cryo-EM and cryo-ET showed that the ATP synthase assembles into cyclic hexamers that further arrange into ~20-MDa pentagonal pyramidal arrays at curved apical inner-membrane regions, an architecture required for normal cristae morphology, as knockout of the linker subunit ATPTG11 disrupted the pyramids and produced aberrant cristae [PMID:33402698]. Beyond its identity as a subunit of this structurally characterized complex, no ATPB-specific mechanistic detail has been characterized in the available corpus.","teleology":[{"year":2018,"claim":"It was unknown how the apicomplexan ATP synthase, including its beta subunit ATPB, was organized; native purification established that the complex exists in defined monomeric and dimeric states and carries an unexpectedly large complement of novel subunits.","evidence":"Partial purification of the native complex followed by mass spectrometry and bioinformatic identification of conserved FO features in T. gondii","pmids":["30005062"],"confidence":"Medium","gaps":["No high-resolution structure of the complex or placement of ATPB within it","No direct functional assay of ATP synthase activity","Role of individual subunits, including ATPB, not tested genetically"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"The three-dimensional architecture and physiological role of the complex were resolved, showing that the ATP synthase forms cyclic hexamers assembling into pentagonal pyramids that dictate cristae shape.","evidence":"Cryo-EM structure of the hexamer, cryo-ET with subtomogram averaging, and genetic knockout of linker subunit ATPTG11 with cristae phenotyping in T. gondii","pmids":["33402698"],"confidence":"High","gaps":["Specific catalytic or structural contribution of ATPB within the hexamer not individually dissected","Consequence of ATPB loss for parasite viability not tested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"A systematic inventory of the complex confirmed and extended the divergent subunit composition, assigning proteins to the F1Fo-ATP synthase and identifying additional uncharacterized subunits.","evidence":"Complexome profiling by blue-native PAGE coupled with quantitative mass spectrometry of T. gondii mitochondria","pmids":["33651838"],"confidence":"Medium","gaps":["Assignment is compositional, not functional, for ATPB","Stoichiometry and assembly order of ATPB not resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Mitochondrial F-type (F1Fo) ATP synthase — monomeric (~600 kDa) and dimeric (>1 MDa) forms, assembling into cyclic hexamers and ~20-MDa pentagonal pyramidal arrays"],"partners":["CORE ATP SYNTHASE SUBUNITS AND FO SUBUNITS A, B, D","IF1 INHIBITOR (BOUND AT DIMER INTERFACE)","CARDIOLIPIN (BOUND AT DIMER INTERFACE)","ATPTG11 (LINKER SUBUNIT OF THE PENTAGONAL PYRAMID ARRAYS)"],"other_free_text":["The complex carries ~17 apicomplexan-specific accessory subunits alongside core subunits, reflecting a highly divergent apicomplexan ATP synthase composition.","The oligomeric architecture of the complex shapes the parasite's tubular cristae at curved apical inner-membrane regions."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"8579614","id":"PMC_8579614","title":"Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum).","date":"1996","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/8579614","citation_count":263,"is_preprint":false},{"pmid":"25879281","id":"PMC_25879281","title":"The NLRP1 inflammasomes.","date":"2015","source":"Immunological reviews","url":"https://pubmed.ncbi.nlm.nih.gov/25879281","citation_count":200,"is_preprint":false},{"pmid":"7744775","id":"PMC_7744775","title":"Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii.","date":"1995","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/7744775","citation_count":146,"is_preprint":false},{"pmid":"8703025","id":"PMC_8703025","title":"Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase.","date":"1996","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/8703025","citation_count":121,"is_preprint":false},{"pmid":"20353694","id":"PMC_20353694","title":"Efficacy and limitations of an ATP-based monitoring system.","date":"2010","source":"Journal of the American Association for Laboratory Animal Science : JAALAS","url":"https://pubmed.ncbi.nlm.nih.gov/20353694","citation_count":95,"is_preprint":false},{"pmid":"33402698","id":"PMC_33402698","title":"ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.","date":"2021","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/33402698","citation_count":78,"is_preprint":false},{"pmid":"19379828","id":"PMC_19379828","title":"Particularities of mitochondrial structure in parasitic protists (Apicomplexa and Kinetoplastida).","date":"2009","source":"The international journal of biochemistry & cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/19379828","citation_count":78,"is_preprint":false},{"pmid":"26001086","id":"PMC_26001086","title":"Metabolic Needs and Capabilities of Toxoplasma gondii through Combined Computational and Experimental Analysis.","date":"2015","source":"PLoS computational biology","url":"https://pubmed.ncbi.nlm.nih.gov/26001086","citation_count":75,"is_preprint":false},{"pmid":"10454205","id":"PMC_10454205","title":"Properties and potential-applications of chemical inhibitors of cyclin-dependent kinases.","date":"1999","source":"Pharmacology & therapeutics","url":"https://pubmed.ncbi.nlm.nih.gov/10454205","citation_count":74,"is_preprint":false},{"pmid":"19464325","id":"PMC_19464325","title":"The role of ATP-binding cassette (ABC) proteins in protozoan parasites.","date":"2009","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/19464325","citation_count":73,"is_preprint":false},{"pmid":"6304058","id":"PMC_6304058","title":"A potent nucleoside triphosphate hydrolase from the parasitic protozoan Toxoplasma gondii. Purification, some properties, and activation by thiol compounds.","date":"1983","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/6304058","citation_count":71,"is_preprint":false},{"pmid":"9575188","id":"PMC_9575188","title":"Induced activation of the Toxoplasma gondii nucleoside triphosphate hydrolase leads to depletion of host cell ATP levels and rapid exit of intracellular parasites from infected cells.","date":"1998","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/9575188","citation_count":63,"is_preprint":false},{"pmid":"26518878","id":"PMC_26518878","title":"Metabolic Cooperation of Glucose and Glutamine Is Essential for the Lytic Cycle of Obligate Intracellular Parasite Toxoplasma gondii.","date":"2015","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/26518878","citation_count":59,"is_preprint":false},{"pmid":"8919992","id":"PMC_8919992","title":"Comparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii.","date":"1996","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/8919992","citation_count":58,"is_preprint":false},{"pmid":"26933036","id":"PMC_26933036","title":"Using a Genetically Encoded Sensor to Identify Inhibitors of Toxoplasma gondii Ca2+ Signaling.","date":"2016","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/26933036","citation_count":54,"is_preprint":false},{"pmid":"33651838","id":"PMC_33651838","title":"Complexome profile of Toxoplasma gondii mitochondria identifies divergent subunits of respiratory chain complexes including new subunits of cytochrome bc1 complex.","date":"2021","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/33651838","citation_count":53,"is_preprint":false},{"pmid":"30005062","id":"PMC_30005062","title":"Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii.","date":"2018","source":"PLoS biology","url":"https://pubmed.ncbi.nlm.nih.gov/30005062","citation_count":38,"is_preprint":false},{"pmid":"30685461","id":"PMC_30685461","title":"Drug Resistance in Protozoan Parasites: An Incessant Wrestle for Survival.","date":"2019","source":"Journal of global antimicrobial resistance","url":"https://pubmed.ncbi.nlm.nih.gov/30685461","citation_count":37,"is_preprint":false},{"pmid":"31091451","id":"PMC_31091451","title":"The Toxoplasma Vacuolar H+-ATPase Regulates Intracellular pH and Impacts the Maturation of Essential Secretory Proteins.","date":"2019","source":"Cell reports","url":"https://pubmed.ncbi.nlm.nih.gov/31091451","citation_count":35,"is_preprint":false},{"pmid":"36302692","id":"PMC_36302692","title":"The mystery of massive mitochondrial complexes: the apicomplexan respiratory chain.","date":"2022","source":"Trends in parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/36302692","citation_count":30,"is_preprint":false},{"pmid":"41789725","id":"PMC_41789725","title":"Unconventional model organisms bend our view on mitochondrial cristae.","date":"2026","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/41789725","citation_count":0,"is_preprint":false},{"pmid":"42313860","id":"PMC_42313860","title":"Inhibition of Toxoplasma gondii proliferation by dimethyl itaconate: Evidence from in vitro and in vivo studies.","date":"2026","source":"PLoS neglected tropical diseases","url":"https://pubmed.ncbi.nlm.nih.gov/42313860","citation_count":0,"is_preprint":false},{"pmid":"41843302","id":"PMC_41843302","title":"Estudo Abrangente do Resveratrol Associado à Sulfadiazina em Linfócitos Infectados com Toxoplasma gondii: Envolvimento da Sinalização Purinérgica na Resposta Imunológica.","date":"2026","source":"Acta parasitologica","url":"https://pubmed.ncbi.nlm.nih.gov/41843302","citation_count":0,"is_preprint":false},{"pmid":"40001505","id":"PMC_40001505","title":"Activity Evaluation and Mode of Action of ICA Against Toxoplasma gondii In Vitro.","date":"2025","source":"Biomolecules","url":"https://pubmed.ncbi.nlm.nih.gov/40001505","citation_count":3,"is_preprint":false},{"pmid":"41427835","id":"PMC_41427835","title":"PI3K/Akt/mTOR signaling pathway mediates energy metabolic reprogramming and regulates mitochondrial homeostasis in host cells exposed to Toxoplasma gondii.","date":"2025","source":"Microbiology spectrum","url":"https://pubmed.ncbi.nlm.nih.gov/41427835","citation_count":2,"is_preprint":false},{"pmid":"40572091","id":"PMC_40572091","title":"Piceatannol Induces Mitochondrial Dysfunction in Toxoplasma gondii.","date":"2025","source":"Microorganisms","url":"https://pubmed.ncbi.nlm.nih.gov/40572091","citation_count":2,"is_preprint":false},{"pmid":"40731026","id":"PMC_40731026","title":"Proline dehydrogenase, a rate-limiting catabolic enzyme, affecting the growth and pathogenicity of Toxoplasma gondii tachyzoites by regulating the proline metabolism and mitochondrial function of the parasite.","date":"2025","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/40731026","citation_count":1,"is_preprint":false},{"pmid":"41193440","id":"PMC_41193440","title":"Structural and functional characterization of TgGSK3, a druggable kinase in Toxoplasma gondii.","date":"2025","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/41193440","citation_count":0,"is_preprint":false},{"pmid":"39878652","id":"PMC_39878652","title":"TgGloL is an atypical glyoxalase/VOC domain-containing apicoplast protein that is important for the growth of Toxoplasma.","date":"2025","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/39878652","citation_count":0,"is_preprint":false},{"pmid":"38589375","id":"PMC_38589375","title":"Metabolic plasticity, essentiality and therapeutic potential of ribose-5-phosphate synthesis in Toxoplasma gondii.","date":"2024","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/38589375","citation_count":11,"is_preprint":false},{"pmid":"39375464","id":"PMC_39375464","title":"Recognition of phylogenetically diverse pathogens through enzymatically amplified recruitment of RNF213.","date":"2024","source":"EMBO reports","url":"https://pubmed.ncbi.nlm.nih.gov/39375464","citation_count":11,"is_preprint":false},{"pmid":"39207139","id":"PMC_39207139","title":"The Toxoplasma gondii mitochondrial transporter ABCB7L is essential for the biogenesis of cytosolic and nuclear iron-sulfur cluster proteins and cytosolic translation.","date":"2024","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/39207139","citation_count":9,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":24792,"output_tokens":1834,"usd":0.050943,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6933,"output_tokens":2888,"usd":0.053433,"stage2_stop_reason":"end_turn"},"total_usd":0.186037,"stage1_batch_id":"msgbatch_015xmQKDRqnTh9anE4m7LiD6","stage2_batch_id":"msgbatch_01JLpkFTVhoQBNgqHCKFrVVU","note":"batch pricing = 50% of standard","corrective_rerun":"2026-09-10 wrong-gene rerun (round-4 rules)","corrective_reason":"re-read with subject anchor"},"stage1_raw":"Looking through the corpus for papers about ATPB (TG_261950), the ATP synthase beta subunit of Toxoplasma gondii.\n\nThe key paper is [9] (PMID:30005062) and [12] (PMID:33402698), which directly study the F-type ATP synthase complex in Toxoplasma/Apicomplexa. Papers [13] (PMID:33651838), [14] (PMID:36302692), and [24] (PMID:41789725) also discuss this complex. ATPB is the beta subunit of this complex.\n\nHowever, I need to be careful: these papers study the ATP synthase *complex* broadly, identifying novel subunits and structures. ATPB itself (the canonical beta subunit) is a core, well-known subunit — the papers focus on the novel/divergent subunits, not on ATPB specifically. None of these papers report a specific experiment targeting ATPB alone.\n\nThe NTPase papers [27], [28], [29], [30], [32] are about nucleoside triphosphate hydrolases — not the ATP synthase beta subunit. These are different proteins entirely.\n\nPapers [9] and [12] study the F-type ATP synthase complex that includes ATPB, and do report complex-level findings. I can record these as complex-level findings where ATPB is a member.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2018,\n      \"finding\": \"The F-type ATP synthase complex of T. gondii, which includes the canonical beta subunit (ATPB), was partially purified in monomeric (~600 kDa) and dimeric (>1 MDa) forms; mass spectrometry identified 20 novel subunits alongside core subunits, and key FO subunits a, b, and d were identified from conserved structural features despite extreme sequence diversification.\",\n      \"method\": \"Partial purification of native complex followed by mass spectrometry; bioinformatic identification of conserved structural features\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — native complex purification with MS identification, single lab, two orthogonal methods (biochemical fractionation + MS)\",\n      \"pmids\": [\"30005062\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"The apicomplexan F-type ATP synthase complex, which includes ATPB, assembles into cyclic hexamers that shape the distinct tubular cristae morphology of T. gondii mitochondria; cryo-EM structure of the hexamer revealed 17 apicomplexan-specific subunits, an extensive dimer interface including bound cardiolipins and inhibitor IF1, and cryo-ET showed hexamers arrange into ~20-MDa pentagonal pyramids at curved apical membrane regions; knockout of linker subunit ATPTG11 disrupted pentagonal pyramids and caused aberrant cristae morphology.\",\n      \"method\": \"Cryo-EM structure determination; cryo-ET with subtomogram averaging; genetic knockout with phenotypic analysis of cristae morphology\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-EM structure plus cryo-ET plus functional genetic knockout, multiple orthogonal methods in one rigorous study\",\n      \"pmids\": [\"33402698\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Complexome profiling of T. gondii mitochondria using a proteomic approach assigned 60 proteins to complexes II, IV, and the F1Fo-ATP synthase (which includes ATPB), identifying 16 previously uncharacterized subunits and establishing the divergent subunit composition of the apicomplexan F1Fo-ATP synthase.\",\n      \"method\": \"Complexome profiling (blue-native PAGE coupled with quantitative mass spectrometry)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — complexome profiling with quantitative MS, single lab, systematic biochemical approach\",\n      \"pmids\": [\"33651838\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"ATPB is the beta subunit of the mitochondrial F-type ATP synthase in Toxoplasma gondii; the complex assembles into cyclic hexamers that form ~20-MDa pentagonal pyramidal arrays at curved apical inner membrane regions, shaping the parasite's distinctive tubular cristae, with the hexamer structure determined by cryo-EM revealing 17 apicomplexan-specific accessory subunits alongside core subunits including cardiolipin and inhibitor IF1 at the dimer interface.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"ATPB is the beta subunit of the divergent mitochondrial F-type (F1Fo) ATP synthase of Toxoplasma gondii, a complex whose organization shapes the parasite's characteristic tubular cristae [#0, #1]. The complex was purified as monomeric (~600 kDa) and dimeric (>1 MDa) native forms, and mass spectrometry, complexome profiling, and cryo-EM together established a highly divergent subunit composition, with core subunits accompanied by roughly 17 apicomplexan-specific accessory subunits, extensively diversified FO subunits a, b, and d, and bound cardiolipins and the inhibitor IF1 at the dimer interface [#0, #1, #2]. Cryo-EM and cryo-ET showed that the ATP synthase assembles into cyclic hexamers that further arrange into ~20-MDa pentagonal pyramidal arrays at curved apical inner-membrane regions, an architecture required for normal cristae morphology, as knockout of the linker subunit ATPTG11 disrupted the pyramids and produced aberrant cristae [#1]. Beyond its identity as a subunit of this structurally characterized complex, no ATPB-specific mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2018,\n      \"claim\": \"It was unknown how the apicomplexan ATP synthase, including its beta subunit ATPB, was organized; native purification established that the complex exists in defined monomeric and dimeric states and carries an unexpectedly large complement of novel subunits.\",\n      \"evidence\": \"Partial purification of the native complex followed by mass spectrometry and bioinformatic identification of conserved FO features in T. gondii\",\n      \"pmids\": [\"30005062\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No high-resolution structure of the complex or placement of ATPB within it\",\n        \"No direct functional assay of ATP synthase activity\",\n        \"Role of individual subunits, including ATPB, not tested genetically\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The three-dimensional architecture and physiological role of the complex were resolved, showing that the ATP synthase forms cyclic hexamers assembling into pentagonal pyramids that dictate cristae shape.\",\n      \"evidence\": \"Cryo-EM structure of the hexamer, cryo-ET with subtomogram averaging, and genetic knockout of linker subunit ATPTG11 with cristae phenotyping in T. gondii\",\n      \"pmids\": [\"33402698\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Specific catalytic or structural contribution of ATPB within the hexamer not individually dissected\",\n        \"Consequence of ATPB loss for parasite viability not tested\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"A systematic inventory of the complex confirmed and extended the divergent subunit composition, assigning proteins to the F1Fo-ATP synthase and identifying additional uncharacterized subunits.\",\n      \"evidence\": \"Complexome profiling by blue-native PAGE coupled with quantitative mass spectrometry of T. gondii mitochondria\",\n      \"pmids\": [\"33651838\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Assignment is compositional, not functional, for ATPB\",\n        \"Stoichiometry and assembly order of ATPB not resolved\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The specific catalytic role, essentiality, and assembly dependencies of ATPB itself remain uncharacterized in the available corpus.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No ATPB-specific genetic knockout or knockdown phenotype\",\n        \"No direct measurement of ATPB contribution to catalysis or complex stability\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0046933\", \"supporting_discovery_ids\": [0, 1, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005743\", \"supporting_discovery_ids\": [1, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0045259\", \"supporting_discovery_ids\": [0, 1, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0015986\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0007007\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"Mitochondrial F-type (F1Fo) ATP synthase — monomeric (~600 kDa) and dimeric (>1 MDa) forms, assembling into cyclic hexamers and ~20-MDa pentagonal pyramidal arrays\"\n    ],\n    \"partners\": [\n      \"Core ATP synthase subunits and FO subunits a, b, d\",\n      \"IF1 inhibitor (bound at dimer interface)\",\n      \"Cardiolipin (bound at dimer interface)\",\n      \"ATPTG11 (linker subunit of the pentagonal pyramid arrays)\"\n    ],\n    \"other_free_text\": [\n      \"The complex carries ~17 apicomplexan-specific accessory subunits alongside core subunits, reflecting a highly divergent apicomplexan ATP synthase composition.\",\n      \"The oligomeric architecture of the complex shapes the parasite's tubular cristae at curved apical inner-membrane regions.\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_261950","name":"ATPB","product":"ATP synthase beta subunit ATP-B","uniprot_acc":"A0A125YYY5","chromosome":"TGME49_chrVIIb","start_pos":1480951},{"strain":"GT1","gene_id":"TGGT1_261950","name":null,"product":"ATP synthase beta subunit ATP-B","uniprot_acc":null,"chromosome":"TGGT1_chrVIIb","start_pos":1457013},{"strain":"RH88","gene_id":"TGRH88_068890","name":null,"product":"ATP synthase beta subunit ATP-B","uniprot_acc":null,"chromosome":"CM023089","start_pos":1501821},{"strain":"VEG","gene_id":"TGVEG_261950","name":null,"product":"ATP synthase beta subunit ATP-B","uniprot_acc":"A0A0F7UVN4","chromosome":"TGVEG_chrVIIb","start_pos":1497583}]}