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단백질커뮤니케이션그룹
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A Dynamic Substrate Pool Revealed by cryo-EM of a Lipid-Preserved Respiratory Supercomplex

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dc.contributor.authorJeon, T.J.-
dc.contributor.authorSeong-Gyu Lee-
dc.contributor.authorYoo, S.H.-
dc.contributor.authorKim, M.-
dc.contributor.authorSong, D.-
dc.contributor.authorRyu, J.-
dc.contributor.authorPark, H.-
dc.contributor.authorKim, D.-S.-
dc.contributor.authorHyun, J.-
dc.contributor.authorHo Min Kim-
dc.contributor.authorRyu, S.E.-
dc.date.accessioned2022-07-29T07:43:07Z-
dc.date.available2022-07-29T07:43:07Z-
dc.date.created2022-07-25-
dc.date.issued2022-06-
dc.identifier.issn1523-0864-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/12017-
dc.description.abstractAims: Mitochondrial respiratory supercomplexes mediate redox electron transfer, generating a proton gradient for ATP synthesis. To provide structural information on the function of supercomplexes in physiologically relevant conditions, we conducted cryoelectron microscopy studies with supercomplexes in a lipid-preserving state. Results: Here, we present cryoelectron microscopy structures of bovine respiratory supercomplex I1III2IV1 by using a lipid-preserving sample preparation. The preparation greatly enhances the intercomplex quinone transfer activity. The structures reveal large intercomplex motions that result in different shapes and sizes of the intercomplex space between complexes I and III, forming a dynamic substrate pool. Biochemical and structural analyses indicated that intercomplex phospholipids mediate the intercomplex motions. An analysis of the different classes of focus-refined complex I showed that structural switches due to quinone reduction led to the formation of a novel channel that could transfer reduced quinones to the intercomplex substrate pool. Innovation and Conclusion: Our results indicate potential mechanism for the facilitated electron transfer involving a dynamic substrate pool and intercomplex movement by which supercomplexes play an active role in the regulation of metabolic flux and reactive oxygen species. Antioxid. Redox Signal. 36, 1101-1118. © 2022, Mary Ann Liebert, Inc., publishers.-
dc.language영어-
dc.publisherMary Ann Liebert Inc.-
dc.titleA Dynamic Substrate Pool Revealed by cryo-EM of a Lipid-Preserved Respiratory Supercomplex-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000808597800001-
dc.identifier.scopusid2-s2.0-85128223353-
dc.identifier.rimsid78592-
dc.contributor.affiliatedAuthorSeong-Gyu Lee-
dc.contributor.affiliatedAuthorHo Min Kim-
dc.identifier.doi10.1089/ars.2021.0114-
dc.identifier.bibliographicCitationAntioxidants and Redox Signaling, v.36, no.16-18, pp.1101 - 1118-
dc.relation.isPartOfAntioxidants and Redox Signaling-
dc.citation.titleAntioxidants and Redox Signaling-
dc.citation.volume36-
dc.citation.number16-18-
dc.citation.startPage1101-
dc.citation.endPage1118-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaEndocrinology & Metabolism-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular BiologyEndocrinology & Metabolism-
dc.subject.keywordPlusMITOCHONDRIAL ELECTRON-TRANSPORT-
dc.subject.keywordPlusCOMPLEX I-
dc.subject.keywordPlusCHAIN-
dc.subject.keywordPlusORGANIZATION-
dc.subject.keywordPlusARCHITECTURE-
dc.subject.keywordPlusMECHANISM-
dc.subject.keywordPlusRESOLUTION-
dc.subject.keywordPlusGEOMETRY-
dc.subject.keywordPlusFLUX-
dc.subject.keywordAuthorcryo-EM structure-
dc.subject.keywordAuthordynamic substrate pool-
dc.subject.keywordAuthorintercomplex movement-
dc.subject.keywordAuthorlipid-preserving state-
dc.subject.keywordAuthorrespiratory supercomplex-
Appears in Collections:
Pioneer Research Center for Biomolecular and Cellular Structure(바이오분자 및 세포구조 연구단) > Protein Communication Group(단백질 커뮤니케이션 그룹) > 1. Journal Papers (저널논문)
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