{"gene":"TG_269442","gene_symbol":"ELC1","run_date":"2026-09-08T14:08:29","timeline":{"discoveries":[{"year":2014,"finding":"TgELC1 binds the MyoA lever arm (neck region) and its presence more than doubles the actin gliding speed of TgMyoA in vitro: TgMyoA heavy chain + TgMLC1 moves actin at ~1.5 µm/s, whereas addition of TgELC1 increases speed to ~3.4 µm/s, demonstrating that ELC1 stabilizes the lever arm to amplify motor displacement.","method":"Baculovirus/Sf9 heterologous expression with TgUNC co-chaperone, purification of TgMyoA complexes, in vitro actin gliding motility assay","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in vitro reconstitution with purified components and quantitative motility assay; single lab but rigorous biochemical reconstitution with clear functional readout","pmids":["25231988"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"finding":"ELC1 and ELC2 are functionally redundant essential light chains of MyoA that are required for parasite invasion, egress, and gliding motility in Toxoplasma. Molecular simulations and point mutations predicted to ablate Ca2+ coordination or the ELC–MLC1 interface impaired gliding quality, displacement, and speed, indicating that Ca2+-dependent stabilization of intermolecular contacts between ELC1/ELC2 and MLC1 within the lever arm promotes productive movement.","method":"Genetic characterization (conditional knockdown/knockout), molecular dynamics simulations, point mutagenesis of Ca2+-binding and ELC–MLC1 interface residues, gliding motility assays, invasion and egress assays","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic loss-of-function with defined phenotypic readout combined with structure-guided mutagenesis validating specific molecular contacts; replicated across two light chains","pmids":["26374117"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"finding":"ELC1 binds to adjacent sites on the MyoA neck (residues 775–818) immediately N-terminal to the MLC1 binding site. Prebinding of MLC1 to the MyoA neck enhances ELC1 affinity 8-fold, Ca2+ coordination by an EF-hand in ELC1 enhances its affinity 7-fold, and together these factors enhance ELC1 binding 49-fold (Kd ~12 nM). Additionally, ELC1 engages the MyoA converter subdomain, coupling the motor domain to the neck for force transduction.","method":"Hydrogen-deuterium exchange mass spectrometry, isothermal titration calorimetry, 1.85 Å crystal structure of MLC1–MyoA peptide complex, binding affinity measurements with full-length MyoA","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure plus HDX-MS and ITC with quantitative binding measurements; multiple orthogonal biophysical methods in a single rigorous study","pmids":["28972141"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"TgELC1 is a component of the glideosome motor complex together with TgMyoA and TgMLC1. Phosphorylation of TgMLC1 (a partner of ELC1 in the complex) is not critical for glideosome assembly or parasite motility, as phospho-mimetic and phospho-null mutants of TgMLC1 had no detectable phenotype.","method":"Phospho-mimetic and phospho-null mutagenesis of TgMLC1, overexpression and allelic replacement, motility assays, complementation in inducible knockout background","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean genetic complementation with phospho-mutants and functional motility readout; finding is negative for MLC1 phosphorylation but confirms ELC1 as a core glideosome component","pmids":["24779470"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"TgELC1/2 together with TgMyoA and TgMLC1 constitute the myosin motor complex. Palmitoylation of TgMLC1 on C8 and C11 mediates MLC1 binding to GAP45; mutations blocking palmitoylation abolish MLC1–GAP45 interaction but have little effect on parasite motility, indicating that ELC1-containing motor complex function is not strictly dependent on MLC1–GAP45 anchorage to the IMC.","method":"Site-directed mutagenesis of TgMLC1 palmitoylation sites (C8, C11), co-immunoprecipitation to assess MLC1–GAP45 interaction, parasite motility assays","journal":"mSphere","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — mutagenesis with Co-IP and motility phenotype in a single lab; contextualizes ELC1 motor complex function in the absence of canonical IMC anchorage","pmids":["34011689"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgELC1 is an essential light chain of the Toxoplasma MyoA glideosome motor that binds the MyoA neck region adjacent to MLC1 and also contacts the converter subdomain; its binding is cooperatively enhanced by Ca2+ coordination through an EF-hand and by prebinding of MLC1, resulting in a high-affinity (~12 nM) complex that stabilizes the lever arm and is required to achieve full actin-gliding speed (~3.4 µm/s) and efficient parasite invasion, egress, and motility."},"narrative":{"mechanistic_narrative":"TgELC1 is an essential light chain of the Toxoplasma gondii MyoA glideosome motor, binding the MyoA neck (lever arm) and stabilizing it to amplify motor displacement [PMID:25231988, PMID:24779470]. In vitro reconstitution shows that adding TgELC1 to the TgMyoA heavy chain–TgMLC1 complex more than doubles actin gliding speed from ~1.5 to ~3.4 µm/s, establishing its role in lever-arm rigidification and force transduction [PMID:25231988]. TgELC1 occupies MyoA neck residues 775–818, immediately N-terminal to the MLC1 site, and its high-affinity engagement (Kd ~12 nM) is cooperatively driven by two factors: prebinding of MLC1 (8-fold enhancement) and Ca2+ coordination via an EF-hand in ELC1 (7-fold enhancement), together giving a 49-fold increase; ELC1 additionally contacts the MyoA converter subdomain, coupling the motor domain to the neck [PMID:28972141]. TgELC1 and its paralog TgELC2 are functionally redundant essential light chains required for parasite invasion, egress, and gliding motility, with Ca2+-dependent stabilization of the ELC–MLC1 interface promoting productive movement [PMID:26374117].","teleology":[{"year":2014,"claim":"Whether ELC1 contributed functionally to the MyoA motor was unknown; reconstitution established that ELC1 stabilizes the lever arm to amplify motor output.","evidence":"Baculovirus/Sf9 expression of TgMyoA complexes with TgUNC co-chaperone and in vitro actin gliding assays showing speed increase from ~1.5 to ~3.4 µm/s upon ELC1 addition","pmids":["25231988"],"confidence":"High","gaps":["Structural basis of lever-arm stabilization not resolved in this study","Contribution of Ca2+ or MLC1 to ELC1 binding not yet dissected"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"The question of whether MLC1 phosphorylation regulates the ELC1-containing glideosome was addressed, confirming ELC1 as a core motor component while ruling out phospho-regulation of MLC1 as essential.","evidence":"Phospho-mimetic/phospho-null mutagenesis of TgMLC1 with allelic replacement and complementation in inducible knockout background, plus motility assays","pmids":["24779470"],"confidence":"Medium","gaps":["Direct role of ELC1 not tested here; finding is centered on the MLC1 partner","Negative result on MLC1 phosphorylation"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"claim":"Whether ELC1 was genetically required for parasite biology was unknown; genetic loss-of-function established ELC1/ELC2 as redundant essential light chains needed for invasion, egress, and motility.","evidence":"Conditional knockdown/knockout, molecular dynamics simulations, and structure-guided point mutagenesis of Ca2+-binding and ELC–MLC1 interface residues with gliding, invasion, and egress assays","pmids":["26374117"],"confidence":"High","gaps":["Precise molecular contacts inferred from simulation rather than experimental structure","Redundancy between ELC1 and ELC2 leaves individual contributions partly unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"claim":"How ELC1 engages MyoA and what drives its affinity were unresolved; biophysical and structural work mapped its binding sites and defined the cooperative determinants of high-affinity assembly.","evidence":"HDX-MS, ITC, and a 1.85 Å crystal structure of the MLC1–MyoA peptide complex with binding measurements on full-length MyoA","pmids":["28972141"],"confidence":"High","gaps":["No direct crystal structure of ELC1 bound to MyoA (ELC1 binding inferred alongside MLC1 structure)","Mechanism by which converter engagement transduces force not fully defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Whether motor function depended on IMC anchorage via the MLC1 partner was tested, showing the ELC1-containing complex retains motility largely independent of MLC1–GAP45 anchoring.","evidence":"Site-directed mutagenesis of TgMLC1 palmitoylation sites (C8, C11), Co-IP of MLC1–GAP45, and parasite motility assays","pmids":["34011689"],"confidence":"Medium","gaps":["ELC1 not directly manipulated; inference about ELC1 complex is indirect","Single-lab Co-IP for the MLC1–GAP45 interaction"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The distinct in vivo contributions of ELC1 versus ELC2, and a direct structure of ELC1 bound to the MyoA neck and converter, remain to be established.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct ELC1–MyoA co-crystal structure","Individual (non-redundant) roles of ELC1 vs ELC2 undefined","Mechanism of converter coupling to force output not experimentally resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Glideosome MyoA motor complex (TgMyoA heavy chain, TgMLC1, TgELC1/ELC2)"],"partners":["TGMYOA (NECK RESIDUES 775–818 AND CONVERTER SUBDOMAIN)","TGMLC1","TGELC2 (REDUNDANT PARALOG)"],"other_free_text":["ELC1 binding to the MyoA neck is cooperatively enhanced ~49-fold (Kd ~12 nM) by MLC1 prebinding (8-fold) and Ca2+ coordination via an EF-hand (7-fold) [#2].","ELC1 addition raises TgMyoA actin gliding speed from ~1.5 to ~3.4 µm/s by stabilizing the lever arm [#0].","ELC1/ELC2 are essential for invasion, egress, and gliding motility [#1]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"26374117","id":"PMC_26374117","title":"Two Essential Light Chains Regulate the MyoA Lever Arm To Promote Toxoplasma Gliding Motility.","date":"2015","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/26374117","citation_count":40,"is_preprint":false},{"pmid":"25231988","id":"PMC_25231988","title":"A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.","date":"2014","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/25231988","citation_count":36,"is_preprint":false},{"pmid":"24779470","id":"PMC_24779470","title":"Assessment of phosphorylation in Toxoplasma glideosome assembly and function.","date":"2014","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/24779470","citation_count":25,"is_preprint":false},{"pmid":"28972141","id":"PMC_28972141","title":"Dissecting the molecular assembly of the Toxoplasma gondii MyoA motility complex.","date":"2017","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/28972141","citation_count":16,"is_preprint":false},{"pmid":"34011689","id":"PMC_34011689","title":"Blocking Palmitoylation of Toxoplasma gondii Myosin Light Chain 1 Disrupts Glideosome Composition but Has Little Impact on Parasite Motility.","date":"2021","source":"mSphere","url":"https://pubmed.ncbi.nlm.nih.gov/34011689","citation_count":11,"is_preprint":false},{"pmid":"30130043","id":"PMC_30130043","title":"[Research Advances on Gliding-associated Proteins of Toxoplasma gondii].","date":"2016","source":"Zhongguo ji sheng chong xue yu ji sheng chong bing za zhi = Chinese journal of parasitology & parasitic diseases","url":"https://pubmed.ncbi.nlm.nih.gov/30130043","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5738,"output_tokens":1721,"usd":0.021514,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6920,"output_tokens":2763,"usd":0.051838,"stage2_stop_reason":"end_turn"},"total_usd":0.073352,"stage1_batch_id":"msgbatch_015xmQKDRqnTh9anE4m7LiD6","stage2_batch_id":"msgbatch_01JLpkFTVhoQBNgqHCKFrVVU","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"TgELC1 binds the MyoA lever arm (neck region) and its presence more than doubles the actin gliding speed of TgMyoA in vitro: TgMyoA heavy chain + TgMLC1 moves actin at ~1.5 µm/s, whereas addition of TgELC1 increases speed to ~3.4 µm/s, demonstrating that ELC1 stabilizes the lever arm to amplify motor displacement.\",\n      \"method\": \"Baculovirus/Sf9 heterologous expression with TgUNC co-chaperone, purification of TgMyoA complexes, in vitro actin gliding motility assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vitro reconstitution with purified components and quantitative motility assay; single lab but rigorous biochemical reconstitution with clear functional readout\",\n      \"pmids\": [\"25231988\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"ELC1 and ELC2 are functionally redundant essential light chains of MyoA that are required for parasite invasion, egress, and gliding motility in Toxoplasma. Molecular simulations and point mutations predicted to ablate Ca2+ coordination or the ELC–MLC1 interface impaired gliding quality, displacement, and speed, indicating that Ca2+-dependent stabilization of intermolecular contacts between ELC1/ELC2 and MLC1 within the lever arm promotes productive movement.\",\n      \"method\": \"Genetic characterization (conditional knockdown/knockout), molecular dynamics simulations, point mutagenesis of Ca2+-binding and ELC–MLC1 interface residues, gliding motility assays, invasion and egress assays\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic loss-of-function with defined phenotypic readout combined with structure-guided mutagenesis validating specific molecular contacts; replicated across two light chains\",\n      \"pmids\": [\"26374117\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"ELC1 binds to adjacent sites on the MyoA neck (residues 775–818) immediately N-terminal to the MLC1 binding site. Prebinding of MLC1 to the MyoA neck enhances ELC1 affinity 8-fold, Ca2+ coordination by an EF-hand in ELC1 enhances its affinity 7-fold, and together these factors enhance ELC1 binding 49-fold (Kd ~12 nM). Additionally, ELC1 engages the MyoA converter subdomain, coupling the motor domain to the neck for force transduction.\",\n      \"method\": \"Hydrogen-deuterium exchange mass spectrometry, isothermal titration calorimetry, 1.85 Å crystal structure of MLC1–MyoA peptide complex, binding affinity measurements with full-length MyoA\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure plus HDX-MS and ITC with quantitative binding measurements; multiple orthogonal biophysical methods in a single rigorous study\",\n      \"pmids\": [\"28972141\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"TgELC1 is a component of the glideosome motor complex together with TgMyoA and TgMLC1. Phosphorylation of TgMLC1 (a partner of ELC1 in the complex) is not critical for glideosome assembly or parasite motility, as phospho-mimetic and phospho-null mutants of TgMLC1 had no detectable phenotype.\",\n      \"method\": \"Phospho-mimetic and phospho-null mutagenesis of TgMLC1, overexpression and allelic replacement, motility assays, complementation in inducible knockout background\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean genetic complementation with phospho-mutants and functional motility readout; finding is negative for MLC1 phosphorylation but confirms ELC1 as a core glideosome component\",\n      \"pmids\": [\"24779470\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"TgELC1/2 together with TgMyoA and TgMLC1 constitute the myosin motor complex. Palmitoylation of TgMLC1 on C8 and C11 mediates MLC1 binding to GAP45; mutations blocking palmitoylation abolish MLC1–GAP45 interaction but have little effect on parasite motility, indicating that ELC1-containing motor complex function is not strictly dependent on MLC1–GAP45 anchorage to the IMC.\",\n      \"method\": \"Site-directed mutagenesis of TgMLC1 palmitoylation sites (C8, C11), co-immunoprecipitation to assess MLC1–GAP45 interaction, parasite motility assays\",\n      \"journal\": \"mSphere\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — mutagenesis with Co-IP and motility phenotype in a single lab; contextualizes ELC1 motor complex function in the absence of canonical IMC anchorage\",\n      \"pmids\": [\"34011689\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgELC1 is an essential light chain of the Toxoplasma MyoA glideosome motor that binds the MyoA neck region adjacent to MLC1 and also contacts the converter subdomain; its binding is cooperatively enhanced by Ca2+ coordination through an EF-hand and by prebinding of MLC1, resulting in a high-affinity (~12 nM) complex that stabilizes the lever arm and is required to achieve full actin-gliding speed (~3.4 µm/s) and efficient parasite invasion, egress, and motility.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TgELC1 is an essential light chain of the Toxoplasma gondii MyoA glideosome motor, binding the MyoA neck (lever arm) and stabilizing it to amplify motor displacement [#0, #3]. In vitro reconstitution shows that adding TgELC1 to the TgMyoA heavy chain–TgMLC1 complex more than doubles actin gliding speed from ~1.5 to ~3.4 µm/s, establishing its role in lever-arm rigidification and force transduction [#0]. TgELC1 occupies MyoA neck residues 775–818, immediately N-terminal to the MLC1 site, and its high-affinity engagement (Kd ~12 nM) is cooperatively driven by two factors: prebinding of MLC1 (8-fold enhancement) and Ca2+ coordination via an EF-hand in ELC1 (7-fold enhancement), together giving a 49-fold increase; ELC1 additionally contacts the MyoA converter subdomain, coupling the motor domain to the neck [#2]. TgELC1 and its paralog TgELC2 are functionally redundant essential light chains required for parasite invasion, egress, and gliding motility, with Ca2+-dependent stabilization of the ELC–MLC1 interface promoting productive movement [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether ELC1 contributed functionally to the MyoA motor was unknown; reconstitution established that ELC1 stabilizes the lever arm to amplify motor output.\",\n      \"evidence\": \"Baculovirus/Sf9 expression of TgMyoA complexes with TgUNC co-chaperone and in vitro actin gliding assays showing speed increase from ~1.5 to ~3.4 µm/s upon ELC1 addition\",\n      \"pmids\": [\"25231988\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of lever-arm stabilization not resolved in this study\", \"Contribution of Ca2+ or MLC1 to ELC1 binding not yet dissected\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"The question of whether MLC1 phosphorylation regulates the ELC1-containing glideosome was addressed, confirming ELC1 as a core motor component while ruling out phospho-regulation of MLC1 as essential.\",\n      \"evidence\": \"Phospho-mimetic/phospho-null mutagenesis of TgMLC1 with allelic replacement and complementation in inducible knockout background, plus motility assays\",\n      \"pmids\": [\"24779470\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct role of ELC1 not tested here; finding is centered on the MLC1 partner\", \"Negative result on MLC1 phosphorylation\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Whether ELC1 was genetically required for parasite biology was unknown; genetic loss-of-function established ELC1/ELC2 as redundant essential light chains needed for invasion, egress, and motility.\",\n      \"evidence\": \"Conditional knockdown/knockout, molecular dynamics simulations, and structure-guided point mutagenesis of Ca2+-binding and ELC–MLC1 interface residues with gliding, invasion, and egress assays\",\n      \"pmids\": [\"26374117\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Precise molecular contacts inferred from simulation rather than experimental structure\", \"Redundancy between ELC1 and ELC2 leaves individual contributions partly unresolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"How ELC1 engages MyoA and what drives its affinity were unresolved; biophysical and structural work mapped its binding sites and defined the cooperative determinants of high-affinity assembly.\",\n      \"evidence\": \"HDX-MS, ITC, and a 1.85 Å crystal structure of the MLC1–MyoA peptide complex with binding measurements on full-length MyoA\",\n      \"pmids\": [\"28972141\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No direct crystal structure of ELC1 bound to MyoA (ELC1 binding inferred alongside MLC1 structure)\", \"Mechanism by which converter engagement transduces force not fully defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Whether motor function depended on IMC anchorage via the MLC1 partner was tested, showing the ELC1-containing complex retains motility largely independent of MLC1–GAP45 anchoring.\",\n      \"evidence\": \"Site-directed mutagenesis of TgMLC1 palmitoylation sites (C8, C11), Co-IP of MLC1–GAP45, and parasite motility assays\",\n      \"pmids\": [\"34011689\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"ELC1 not directly manipulated; inference about ELC1 complex is indirect\", \"Single-lab Co-IP for the MLC1–GAP45 interaction\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The distinct in vivo contributions of ELC1 versus ELC2, and a direct structure of ELC1 bound to the MyoA neck and converter, remain to be established.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No direct ELC1–MyoA co-crystal structure\", \"Individual (non-redundant) roles of ELC1 vs ELC2 undefined\", \"Mechanism of converter coupling to force output not experimentally resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0017022\", \"supporting_discovery_ids\": [0, 2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005509\", \"supporting_discovery_ids\": [1, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0016460\", \"supporting_discovery_ids\": [0, 3, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0071976\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\"Glideosome MyoA motor complex (TgMyoA heavy chain, TgMLC1, TgELC1/ELC2)\"],\n    \"partners\": [\"TgMyoA (neck residues 775–818 and converter subdomain)\", \"TgMLC1\", \"TgELC2 (redundant paralog)\"],\n    \"other_free_text\": [\n      \"ELC1 binding to the MyoA neck is cooperatively enhanced ~49-fold (Kd ~12 nM) by MLC1 prebinding (8-fold) and Ca2+ coordination via an EF-hand (7-fold) [#2].\",\n      \"ELC1 addition raises TgMyoA actin gliding speed from ~1.5 to ~3.4 µm/s by stabilizing the lever arm [#0].\",\n      \"ELC1/ELC2 are essential for invasion, egress, and gliding motility [#1].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_269442","name":"ELC1","product":"essential light chain ELC1","uniprot_acc":"A0A125YUL9","chromosome":"TGME49_chrVIII","start_pos":5796271},{"strain":"GT1","gene_id":"TGGT1_269442","name":null,"product":"putative calmodulin","uniprot_acc":null,"chromosome":"TGGT1_chrVIII","start_pos":5794616},{"strain":"RH88","gene_id":"TGRH88_081780","name":null,"product":"putative calmodulin","uniprot_acc":null,"chromosome":"CM023089","start_pos":10914615},{"strain":"VEG","gene_id":"TGVEG_269442","name":null,"product":"putative calmodulin","uniprot_acc":"A0A125YUM0","chromosome":"TGVEG_chrVIII","start_pos":5811410}]}