{"gene":"PF3D7_0719600","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2014,"finding":"PF3D7_0719600 (L11a) was resolved as a component of the P. falciparum 80S ribosome in the first cryo-EM structure of this ribosome at 3.2 Å resolution; the structure established membership of L11a in the large (60S) ribosomal subunit of the P. falciparum cytoplasmic ribosome.","method":"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM structure, but the abstract reports the ribosome complex overall and does not isolate or functionally validate L11a specifically; single study","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"PF3D7_0719600 (L11a) was identified as a structural component of the P. falciparum 80S ribosome through five cryo-EM reconstructions of ribosomes purified from blood-stage schizonts at sub-nanometer resolution, with atomic models built by flexible fitting.","method":"Cryo-EM reconstruction and atomic model building from P. falciparum schizont-purified ribosomes","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — multiple cryo-EM reconstructions with atomic modeling, but L11a is not individually characterized beyond complex membership; single lab","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"PF3D7_0719600 (L11a) is a constituent of the P. falciparum 80S ribosome structural context resolved at 3.2 Å by cryo-EM, within which the GTPase-associated centre (on the large subunit) was identified as the binding site for mefloquine.","method":"Cryo-EM structure at 3.2 Å; mutagenesis of ribosome-binding residues to confirm drug mechanism","journal":"Nature microbiology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — rigorous cryo-EM plus mutagenesis, but L11a is not individually functionally characterized; findings are for the ribosome complex as a whole","pmids":["28288098"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"PF3D7_0719600 (L11a) is a structural component of the native P. falciparum 80S ribosome visualized in actively translating states inside infected human erythrocytes by in situ cryo-electron tomography; eight high-resolution structures of the ribosome in elongation states were determined, placing L11a in its native cellular context during active translation.","method":"In situ cryo-electron tomography of P. falciparum-infected human erythrocytes; eight high-resolution ribosome structures in translating states","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — state-of-the-art in situ structural approach with multiple structures, but L11a is not individually characterized beyond its role as a ribosomal component; single study","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0719600 (L11a) is a component of the large (60S) subunit of the P. falciparum cytoplasmic 80S ribosome, as established by multiple cryo-EM and in situ cryo-ET structural studies; beyond its membership in this complex, no specific enzymatic activity, binding partner, post-translational modification, or individual functional role has been mechanistically established for L11a itself in the available literature."},"narrative":{"mechanistic_narrative":"PF3D7_0719600 (L11a) is a structural component of the large (60S) subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, established by successive cryo-EM structures of the purified ribosome [PMID:24913268, PMID:26432834] and confirmed in the native context of actively translating ribosomes inside infected human erythrocytes by in situ cryo-electron tomography [PMID:40825879]. Within these structures the 80S ribosome harbors a druggable GTPase-associated centre on the large subunit that serves as the mefloquine binding site, though this drug-binding role is attributed to the large subunit as a whole rather than to L11a specifically [PMID:28288098]. Beyond its membership in the 60S subunit as resolved by these structural studies, no specific enzymatic activity, binding partner, post-translational modification, or individual functional role has been mechanistically established for L11a itself in the available corpus.","teleology":[{"year":2014,"claim":"Whether L11a is a bona fide constituent of the P. falciparum ribosome was first answered by resolving it within a high-resolution structure of the assembled 80S ribosome, placing it in the large (60S) subunit.","evidence":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution","pmids":["24913268"],"confidence":"Medium","gaps":["L11a is resolved only as part of the complex and is not individually isolated or functionally validated","No enzymatic activity or specific binding partner assigned to L11a itself"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"The assignment of L11a to the 60S subunit was corroborated across multiple ribosome conformations purified from blood-stage parasites, strengthening its status as a stable structural component.","evidence":"Five cryo-EM reconstructions with flexibly fitted atomic models from schizont-purified ribosomes","pmids":["26432834"],"confidence":"Medium","gaps":["L11a not characterized beyond complex membership","No stage-specific or functional role distinguished for L11a"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"Placing L11a within a structure that also mapped the antimalarial mefloquine binding site clarified that the druggable GTPase-associated centre lies on the large subunit, but did not attribute this drug interaction to L11a itself.","evidence":"Cryo-EM structure at 3.2 Å with mutagenesis of ribosome-binding residues to confirm the mefloquine mechanism","pmids":["28288098"],"confidence":"Medium","gaps":["Drug binding is a property of the large subunit, not demonstrated to involve L11a specifically","No direct L11a-mefloquine contact established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether L11a occupies the same position in functioning ribosomes in vivo was addressed by visualizing native, actively translating 80S ribosomes inside infected erythrocytes, confirming L11a in its cellular context during elongation.","evidence":"In situ cryo-electron tomography of P. falciparum-infected human erythrocytes yielding eight ribosome structures in translating elongation states","pmids":["40825879"],"confidence":"Medium","gaps":["L11a is resolved only as a ribosomal component, not individually characterized","No functional contribution of L11a to elongation dynamics isolated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"No experiment in the available corpus assigns L11a an individual molecular activity, binding partner, post-translational modification, or non-structural function distinct from its membership in the 60S subunit.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No genetic or biochemical dissection of L11a-specific function","No interaction partners beyond the ribosome established for L11a","No post-translational modification or regulatory role characterized"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["P. falciparum cytoplasmic 80S ribosome (large 60S subunit)"],"partners":[],"other_free_text":["L11a is resolved only as a structural component of the P. falciparum 80S ribosome across cryo-EM and in situ cryo-ET studies; the corpus establishes nothing about L11a beyond its membership in this complex.","The mefloquine binding site (GTPase-associated centre) is attributed to the large ribosomal subunit as a whole, not to L11a specifically [#2]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"24913268","id":"PMC_24913268","title":"Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine.","date":"2014","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/24913268","citation_count":272,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28288098","id":"PMC_28288098","title":"Mefloquine targets the Plasmodium falciparum 80S ribosome to inhibit protein synthesis.","date":"2017","source":"Nature microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/28288098","citation_count":136,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26432834","id":"PMC_26432834","title":"Dynamical features of the Plasmodium falciparum ribosome during translation.","date":"2015","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/26432834","citation_count":45,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40825879","id":"PMC_40825879","title":"Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug.","date":"2025","source":"Nature structural & molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/40825879","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40480224","id":"PMC_40480224","title":"Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome.","date":"2025","source":"Structure (London, England : 1993)","url":"https://pubmed.ncbi.nlm.nih.gov/40480224","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4839,"output_tokens":1178,"usd":0.016094,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5963,"output_tokens":2127,"usd":0.041495,"stage2_stop_reason":"end_turn"},"total_usd":0.057589,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"PF3D7_0719600 (L11a) was resolved as a component of the P. falciparum 80S ribosome in the first cryo-EM structure of this ribosome at 3.2 Å resolution; the structure established membership of L11a in the large (60S) ribosomal subunit of the P. falciparum cytoplasmic ribosome.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM structure, but the abstract reports the ribosome complex overall and does not isolate or functionally validate L11a specifically; single study\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"PF3D7_0719600 (L11a) was identified as a structural component of the P. falciparum 80S ribosome through five cryo-EM reconstructions of ribosomes purified from blood-stage schizonts at sub-nanometer resolution, with atomic models built by flexible fitting.\",\n      \"method\": \"Cryo-EM reconstruction and atomic model building from P. falciparum schizont-purified ribosomes\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — multiple cryo-EM reconstructions with atomic modeling, but L11a is not individually characterized beyond complex membership; single lab\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"PF3D7_0719600 (L11a) is a constituent of the P. falciparum 80S ribosome structural context resolved at 3.2 Å by cryo-EM, within which the GTPase-associated centre (on the large subunit) was identified as the binding site for mefloquine.\",\n      \"method\": \"Cryo-EM structure at 3.2 Å; mutagenesis of ribosome-binding residues to confirm drug mechanism\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — rigorous cryo-EM plus mutagenesis, but L11a is not individually functionally characterized; findings are for the ribosome complex as a whole\",\n      \"pmids\": [\"28288098\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"PF3D7_0719600 (L11a) is a structural component of the native P. falciparum 80S ribosome visualized in actively translating states inside infected human erythrocytes by in situ cryo-electron tomography; eight high-resolution structures of the ribosome in elongation states were determined, placing L11a in its native cellular context during active translation.\",\n      \"method\": \"In situ cryo-electron tomography of P. falciparum-infected human erythrocytes; eight high-resolution ribosome structures in translating states\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — state-of-the-art in situ structural approach with multiple structures, but L11a is not individually characterized beyond its role as a ribosomal component; single study\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0719600 (L11a) is a component of the large (60S) subunit of the P. falciparum cytoplasmic 80S ribosome, as established by multiple cryo-EM and in situ cryo-ET structural studies; beyond its membership in this complex, no specific enzymatic activity, binding partner, post-translational modification, or individual functional role has been mechanistically established for L11a itself in the available literature.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0719600 (L11a) is a structural component of the large (60S) subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, established by successive cryo-EM structures of the purified ribosome [#0, #1] and confirmed in the native context of actively translating ribosomes inside infected human erythrocytes by in situ cryo-electron tomography [#3]. Within these structures the 80S ribosome harbors a druggable GTPase-associated centre on the large subunit that serves as the mefloquine binding site, though this drug-binding role is attributed to the large subunit as a whole rather than to L11a specifically [#2]. Beyond its membership in the 60S subunit as resolved by these structural studies, no specific enzymatic activity, binding partner, post-translational modification, or individual functional role has been mechanistically established for L11a itself in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether L11a is a bona fide constituent of the P. falciparum ribosome was first answered by resolving it within a high-resolution structure of the assembled 80S ribosome, placing it in the large (60S) subunit.\",\n      \"evidence\": \"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution\",\n      \"pmids\": [\n        \"24913268\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"L11a is resolved only as part of the complex and is not individually isolated or functionally validated\",\n        \"No enzymatic activity or specific binding partner assigned to L11a itself\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Plasmodium falciparum\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"The assignment of L11a to the 60S subunit was corroborated across multiple ribosome conformations purified from blood-stage parasites, strengthening its status as a stable structural component.\",\n      \"evidence\": \"Five cryo-EM reconstructions with flexibly fitted atomic models from schizont-purified ribosomes\",\n      \"pmids\": [\n        \"26432834\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"L11a not characterized beyond complex membership\",\n        \"No stage-specific or functional role distinguished for L11a\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Plasmodium falciparum\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Placing L11a within a structure that also mapped the antimalarial mefloquine binding site clarified that the druggable GTPase-associated centre lies on the large subunit, but did not attribute this drug interaction to L11a itself.\",\n      \"evidence\": \"Cryo-EM structure at 3.2 Å with mutagenesis of ribosome-binding residues to confirm the mefloquine mechanism\",\n      \"pmids\": [\n        \"28288098\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Drug binding is a property of the large subunit, not demonstrated to involve L11a specifically\",\n        \"No direct L11a-mefloquine contact established\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Plasmodium falciparum\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether L11a occupies the same position in functioning ribosomes in vivo was addressed by visualizing native, actively translating 80S ribosomes inside infected erythrocytes, confirming L11a in its cellular context during elongation.\",\n      \"evidence\": \"In situ cryo-electron tomography of P. falciparum-infected human erythrocytes yielding eight ribosome structures in translating elongation states\",\n      \"pmids\": [\n        \"40825879\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"L11a is resolved only as a ribosomal component, not individually characterized\",\n        \"No functional contribution of L11a to elongation dynamics isolated\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Plasmodium falciparum\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"No experiment in the available corpus assigns L11a an individual molecular activity, binding partner, post-translational modification, or non-structural function distinct from its membership in the 60S subunit.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No genetic or biochemical dissection of L11a-specific function\",\n        \"No interaction partners beyond the ribosome established for L11a\",\n        \"No post-translational modification or regulatory role characterized\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Plasmodium falciparum\",\n          \"strain\": \"\"\n        }\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\n        \"term_id\": \"GO:0003735\",\n        \"supporting_discovery_ids\": [\n          0,\n          1,\n          3\n        ]\n      }\n    ],\n    \"localization\": [\n      {\n        \"term_id\": \"GO:0022625\",\n        \"supporting_discovery_ids\": [\n          0,\n          1,\n          2,\n          3\n        ]\n      },\n      {\n        \"term_id\": \"GO:0005737\",\n        \"supporting_discovery_ids\": [\n          3\n        ]\n      }\n    ],\n    \"pathway\": [\n      {\n        \"term_id\": \"GO:0006414\",\n        \"supporting_discovery_ids\": [\n          3\n        ]\n      }\n    ],\n    \"complexes\": [\n      \"P. falciparum cytoplasmic 80S ribosome (large 60S subunit)\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"L11a is resolved only as a structural component of the P. falciparum 80S ribosome across cryo-EM and in situ cryo-ET studies; the corpus establishes nothing about L11a beyond its membership in this complex.\",\n      \"The mefloquine binding site (GTPase-associated centre) is attributed to the large ribosomal subunit as a whole, not to L11a specifically [#2].\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0719600","name":null,"product":"60S ribosomal protein L11a, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0617100","name":null,"product":"60S ribosomal protein L11a, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0315000","name":null,"product":"60S ribosomal protein L11a, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}