{"gene":"PF3D7_1308300","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2014,"finding":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the structural context of the small (40S) subunit, within which RPS27 (PF3D7_1308300) is a constituent protein; the structure established that emetine binds the E-site of the small subunit to block mRNA/tRNA translocation.","method":"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM structure of the intact ribosome, but RPS27 itself is only implicitly part of the small subunit and is not individually interrogated or mutagenized; single study","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Five cryo-EM reconstructions of P. falciparum blood-stage schizont ribosomes at sub-nanometer resolution, with atomic models built by flexible fitting, established structural and dynamic features of the 80S ribosome (including the 40S small subunit where RPS27/PF3D7_1308300 resides) that differentiate it from mammalian ribosomes.","method":"Cryo-EM with flexible-fitting atomic model building from blood-stage schizont ribosomes; five reconstructions capturing different translational states","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — multiple cryo-EM structures with atomic models, but RPS27 is not individually interrogated; single lab study","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"Eight high-resolution in situ cryo-electron tomography structures of the native P. falciparum ribosome in actively translating states inside infected erythrocytes were determined, establishing the molecular architecture of the malarial translation elongation cycle; RPS27/PF3D7_1308300 is a structural component of the 40S small subunit visible in these native complexes.","method":"In situ cryo-electron tomography at high resolution inside P. falciparum-infected human erythrocytes; eight structures of actively translating ribosomes","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — rigorous in situ structural biology establishing native ribosome architecture, but RPS27 itself is not individually mutated or functionally dissected; single study","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"RPS27 (PF3D7_1308300) is a structural component of the P. falciparum 40S ribosomal small subunit, whose overall architecture and translational dynamics have been resolved by multiple cryo-EM and cryo-ET studies; no experiment has yet individually interrogated the specific molecular function, interactions, or post-translational modifications of RPS27 itself beyond its membership in the 80S ribosome complex."},"narrative":{"mechanistic_narrative":"RPS27 (PF3D7_1308300) is a constituent protein of the 40S small subunit of the Plasmodium falciparum 80S ribosome, resolved as part of the assembled particle by successive cryo-EM and in situ cryo-electron tomography studies [PMID:24913268, PMID:40825879]. It is present within the small subunit architecture visualized in the intact ribosome, including native, actively translating ribosomes captured inside infected erythrocytes and states that differentiate the malarial ribosome from its mammalian counterpart [PMID:26432834, PMID:40825879]. Beyond this structural membership in the 80S ribosome, the specific molecular function, interactions, and post-translational modifications of RPS27 itself have not been individually interrogated in the available corpus; every finding derives from whole-ribosome structural work in which RPS27 was not separately mutated or functionally dissected.","teleology":[{"year":2014,"claim":"Establishing the first high-resolution structure of the intact malarial ribosome placed the 40S small subunit — and therefore RPS27 as one of its component proteins — in defined structural context and showed how a translation inhibitor engages the small subunit.","evidence":"Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome bound to emetine, which occupies the small-subunit E-site to block translocation","pmids":["24913268"],"confidence":"Medium","gaps":["RPS27 is only implicitly part of the small subunit and is not individually interrogated or mutagenized","No RPS27-specific function, contact, or dynamics resolved","Single study"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Capturing multiple translational states of the blood-stage ribosome defined dynamic features of the 40S subunit that distinguish the parasite ribosome from the mammalian one, refining the structural environment in which RPS27 sits.","evidence":"Five cryo-EM reconstructions of schizont-stage 80S ribosomes at sub-nanometer resolution with flexible-fitting atomic models","pmids":["26432834"],"confidence":"Medium","gaps":["RPS27 is not individually interrogated within the small subunit","No functional role attributed specifically to RPS27","Single lab study"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Resolving native, actively translating ribosomes in situ established the molecular architecture of the malarial elongation cycle and confirmed RPS27 as a structural component of the 40S subunit in physiologically translating complexes rather than only purified particles.","evidence":"In situ cryo-electron tomography yielding eight high-resolution structures of translating ribosomes inside P. falciparum-infected human erythrocytes","pmids":["40825879"],"confidence":"Medium","gaps":["RPS27 itself is not individually mutated or functionally dissected","No RPS27-specific interactions or modifications resolved","Single study"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether RPS27 has any function, interaction, or regulatory role independent of its structural incorporation into the 40S subunit remains entirely unaddressed.","evidence":"No experiment in the corpus individually perturbs, deletes, tags, or biochemically isolates RPS27","pmids":[],"confidence":"Low","gaps":["No genetic knockout, knockdown, or complementation of RPS27","No assembly, extra-ribosomal, or post-translational modification data specific to RPS27","No direct interaction partners established beyond ribosome membership"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["40S ribosomal small subunit","P. falciparum 80S ribosome"],"partners":[],"other_free_text":["RPS27 (PF3D7_1308300) is characterized in the corpus only as a structural component of the 40S small subunit of the P. falciparum 80S ribosome; no experiment individually interrogates its molecular function, specific interactions, or post-translational modifications.","Structural context established by whole-ribosome cryo-EM and in situ cryo-electron tomography [#0, #1, #2]; emetine binding to the small-subunit E-site was resolved in the same 80S structure but is not an RPS27-specific interaction [#0]."]}},"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":276,"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":46,"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":10,"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":4,"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":4452,"output_tokens":958,"usd":0.013863,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5666,"output_tokens":1852,"usd":0.037315,"stage2_stop_reason":"end_turn"},"total_usd":0.051178,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the structural context of the small (40S) subunit, within which RPS27 (PF3D7_1308300) is a constituent protein; the structure established that emetine binds the E-site of the small subunit to block mRNA/tRNA translocation.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM structure of the intact ribosome, but RPS27 itself is only implicitly part of the small subunit and is not individually interrogated or mutagenized; single study\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Five cryo-EM reconstructions of P. falciparum blood-stage schizont ribosomes at sub-nanometer resolution, with atomic models built by flexible fitting, established structural and dynamic features of the 80S ribosome (including the 40S small subunit where RPS27/PF3D7_1308300 resides) that differentiate it from mammalian ribosomes.\",\n      \"method\": \"Cryo-EM with flexible-fitting atomic model building from blood-stage schizont ribosomes; five reconstructions capturing different translational states\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — multiple cryo-EM structures with atomic models, but RPS27 is not individually interrogated; single lab study\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Eight high-resolution in situ cryo-electron tomography structures of the native P. falciparum ribosome in actively translating states inside infected erythrocytes were determined, establishing the molecular architecture of the malarial translation elongation cycle; RPS27/PF3D7_1308300 is a structural component of the 40S small subunit visible in these native complexes.\",\n      \"method\": \"In situ cryo-electron tomography at high resolution inside P. falciparum-infected human erythrocytes; eight structures of actively translating ribosomes\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — rigorous in situ structural biology establishing native ribosome architecture, but RPS27 itself is not individually mutated or functionally dissected; single study\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"RPS27 (PF3D7_1308300) is a structural component of the P. falciparum 40S ribosomal small subunit, whose overall architecture and translational dynamics have been resolved by multiple cryo-EM and cryo-ET studies; no experiment has yet individually interrogated the specific molecular function, interactions, or post-translational modifications of RPS27 itself beyond its membership in the 80S ribosome complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RPS27 (PF3D7_1308300) is a constituent protein of the 40S small subunit of the Plasmodium falciparum 80S ribosome, resolved as part of the assembled particle by successive cryo-EM and in situ cryo-electron tomography studies [#0, #2]. It is present within the small subunit architecture visualized in the intact ribosome, including native, actively translating ribosomes captured inside infected erythrocytes and states that differentiate the malarial ribosome from its mammalian counterpart [#1, #2]. Beyond this structural membership in the 80S ribosome, the specific molecular function, interactions, and post-translational modifications of RPS27 itself have not been individually interrogated in the available corpus; every finding derives from whole-ribosome structural work in which RPS27 was not separately mutated or functionally dissected.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing the first high-resolution structure of the intact malarial ribosome placed the 40S small subunit — and therefore RPS27 as one of its component proteins — in defined structural context and showed how a translation inhibitor engages the small subunit.\",\n      \"evidence\": \"Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome bound to emetine, which occupies the small-subunit E-site to block translocation\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"RPS27 is only implicitly part of the small subunit and is not individually interrogated or mutagenized\",\n        \"No RPS27-specific function, contact, or dynamics resolved\",\n        \"Single study\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Capturing multiple translational states of the blood-stage ribosome defined dynamic features of the 40S subunit that distinguish the parasite ribosome from the mammalian one, refining the structural environment in which RPS27 sits.\",\n      \"evidence\": \"Five cryo-EM reconstructions of schizont-stage 80S ribosomes at sub-nanometer resolution with flexible-fitting atomic models\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"RPS27 is not individually interrogated within the small subunit\",\n        \"No functional role attributed specifically to RPS27\",\n        \"Single lab study\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Resolving native, actively translating ribosomes in situ established the molecular architecture of the malarial elongation cycle and confirmed RPS27 as a structural component of the 40S subunit in physiologically translating complexes rather than only purified particles.\",\n      \"evidence\": \"In situ cryo-electron tomography yielding eight high-resolution structures of translating ribosomes inside P. falciparum-infected human erythrocytes\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"RPS27 itself is not individually mutated or functionally dissected\",\n        \"No RPS27-specific interactions or modifications resolved\",\n        \"Single study\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether RPS27 has any function, interaction, or regulatory role independent of its structural incorporation into the 40S subunit remains entirely unaddressed.\",\n      \"evidence\": \"No experiment in the corpus individually perturbs, deletes, tags, or biochemically isolates RPS27\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No genetic knockout, knockdown, or complementation of RPS27\",\n        \"No assembly, extra-ribosomal, or post-translational modification data specific to RPS27\",\n        \"No direct interaction partners established beyond ribosome membership\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003735\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0022627\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006412\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"complexes\": [\n      \"40S ribosomal small subunit\",\n      \"P. falciparum 80S ribosome\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"RPS27 (PF3D7_1308300) is characterized in the corpus only as a structural component of the 40S small subunit of the P. falciparum 80S ribosome; no experiment individually interrogates its molecular function, specific interactions, or post-translational modifications.\",\n      \"Structural context established by whole-ribosome cryo-EM and in situ cryo-electron tomography [#0, #1, #2]; emetine binding to the small-subunit E-site was resolved in the same 80S structure but is not an RPS27-specific interaction [#0].\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1308300","name":null,"product":"40S ribosomal protein S27","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1406800","name":null,"product":"40S ribosomal protein S27, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1408700","name":null,"product":"40S ribosomal protein S27, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"RPS27","evaluation":null}