| http://purl.uniprot.org/citations/36952377 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/36952377 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/36952377 | http://www.w3.org/2000/01/rdf-schema#comment | "Respiratory complex I is a proton-pumping oxidoreductase key to bioenergetic metabolism. Biochemical studies have found a divide in the behavior of complex I in metazoans that aligns with the evolutionary split between Protostomia and Deuterostomia. Complex I from Deuterostomia including mammals can adopt a biochemically defined off-pathway 'deactive' state, whereas complex I from Protostomia cannot. The presence of off-pathway states complicates the interpretation of structural results and has led to considerable mechanistic debate. Here, we report the structure of mitochondrial complex I from the thoracic muscles of the model protostome Drosophila melanogaster. We show that although D. melanogaster complex I (Dm-CI) does not have a NEM-sensitive deactive state, it does show slow activation kinetics indicative of an off-pathway resting state. The resting-state structure of Dm-CI from the thoracic muscle reveals multiple conformations. We identify a helix-locked state in which an N-terminal α-helix on the NDUFS4 subunit wedges between the peripheral and membrane arms. Comparison of the Dm-CI structure and conformational states to those observed in bacteria, yeast, and mammals provides insight into the roles of subunits across organisms, explains why the Dm-CI off-pathway resting state is NEM insensitive, and raises questions regarding current mechanistic models of complex I turnover."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.84415"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.84415"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Letts J.A."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Letts J.A."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Owusu-Ansah E."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Owusu-Ansah E."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Padavannil A."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Padavannil A."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Murari A."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Murari A."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Rhooms S.K."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/author | "Rhooms S.K."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/name | "Elife"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/name | "Elife"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/pages | "e84415"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/pages | "e84415"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/title | "Resting mitochondrial complex I from Drosophila melanogaster adopts a helix-locked state."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/title | "Resting mitochondrial complex I from Drosophila melanogaster adopts a helix-locked state."xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/36952377 | http://purl.uniprot.org/core/volume | "12"xsd:string |