{"id":"84bebed0-39c2-585e-8946-edc15d3a37a7","stable_key":"335be270-ea4a-5c8e-ad04-964fd22a439e:vanadium-f1-transition","predicate":"stabilizes_adp_mg_complex","statement":"Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"f916a232-ceed-50da-8228-bc1d090c51e2","mechanism_event_label":"Another ATP-handling enzyme can bind the phosphate analogue.","subject":{"id":"bef86a6e-28a0-5df9-9306-3f05991aa159","slug":"vanadate-v","display_name":"Vanadate(V), protonation/speciation dependent","entity_type_key":"chemical_species"},"object":{"id":"4a13ce7c-7e52-543c-90d2-d1bc2a1ce1b2","slug":"rat-liver-f1-atp-synthase","display_name":"Rat liver F1 ATP synthase catalytic unit","entity_type_key":"protein_complex"},"evidence_count":1,"mechanism_event":{"id":"f916a232-ceed-50da-8228-bc1d090c51e2","stable_key":"335be270-ea4a-5c8e-ad04-964fd22a439e:vanadium-f1-transition-event","event_type":"observed_relationship","label":"Another ATP-handling enzyme can bind the phosphate analogue.","description":"Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"bef86a6e-28a0-5df9-9306-3f05991aa159","slug":"vanadate-v","display_name":"Vanadate(V), protonation/speciation dependent","entity_type_key":"chemical_species"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"4a13ce7c-7e52-543c-90d2-d1bc2a1ce1b2","slug":"rat-liver-f1-atp-synthase","display_name":"Rat liver F1 ATP synthase catalytic unit","entity_type_key":"protein_complex"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c5cbad45-22c6-594b-ab6b-71880dab1b24","slug":"vanadium","display_name":"Vanadium","entity_type_key":"nutrient_element"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"136c3764-1b93-5f79-8673-9001cab9bc3d","slug":"adp","display_name":"Adenosine diphosphate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"b28dfc54-a5ef-5f9e-ac1f-890b68e58dc3","slug":"inorganic-phosphate","display_name":"Inorganic phosphate","entity_type_key":"chemical_species"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""},{"entity":{"id":"58b974f1-d389-5bf6-81cd-889c44442c42","slug":"atp","display_name":"ATP","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":6,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Rat liver F1 crystallography.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A captured structure is not proof that a given oral dose suppresses mitochondrial ATP production.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vanadium","display_name":"Vanadium","entity_type_key":"nutrient_element"}},{"dimension":"plain_language","value_text":"Another ATP-handling enzyme can bind the phosphate analogue.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16531409/ · DOI 10.1074/jbc.M513369200","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a41cc7de-e387-5b60-b65a-830081b16f7e","evidence_kind":"source_excerpt","locator":"Lines 262-268","start_line":262,"end_line":268,"excerpt":"## vanadium-f1-transition\nAnother ATP-handling enzyme can bind the phosphate analogue.\nVanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region.\nModel: Rat liver F1 crystallography.\nLimitations: A captured structure is not proof that a given oral dose suppresses mitochondrial ATP production.\nEvidence access: Primary abstract\nMitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16531409/ · DOI 10.1074/jbc.M513369200","model_system":"Rat liver F1 crystallography.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"e4d5d0ba-529b-540f-96ed-e719d116ccfd","stable_key":"import-335be270-ea4a-5c8e-ad04-964fd22a439e","title":"Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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