Maturation of the respiratory complex II flavoprotein.


Journal

Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784

Informations de publication

Date de publication:
12 2019
Historique:
received: 29 01 2019
accepted: 31 01 2019
pubmed: 10 3 2019
medline: 4 8 2020
entrez: 10 3 2019
Statut: ppublish

Résumé

Respiratory complexes are complicated multi-subunit cofactor-containing machines that allow cells to harvest energy from the environment. Maturation of these complexes requires protein folding, cofactor insertion, and assembly of multiple subunits into a final, functional complex. Because the intermediate states in complex maturation are transitory, these processes are poorly understood. This review gives an overview of the process of maturation in respiratory complex II with a focus on recent structural studies on intermediates formed during covalent flavinylation of the catalytic subunit, SDHA. Covalent flavinylation has an evolutionary significance because variants of complex II enzymes with the covalent ligand removed by mutagenesis cannot oxidize succinate, but can still perform the reverse reaction and reduce fumarate. Since succinate oxidation is a key step of aerobic respiration, the covalent bond of complex II appears to be important for aerobic life.

Identifiants

pubmed: 30851631
pii: S0959-440X(18)30142-8
doi: 10.1016/j.sbi.2019.01.027
pmc: PMC6731172
mid: NIHMS1523364
pii:
doi:

Substances chimiques

Electron Transport Chain Complex Proteins 0
Flavoproteins 0
Protein Subunits 0
respiratory complex II 0
Flavin-Adenine Dinucleotide 146-14-5
Electron Transport Complex II EC 1.3.5.1
SDHA protein, human EC 1.3.5.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

38-46

Subventions

Organisme : BLRD VA
ID : IK6 BX004215
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK058404
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM061606
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

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Auteurs

Pankaj Sharma (P)

Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, United States.

Elena Maklashina (E)

Molecular Biology Division, San Francisco VA Health Care System, San Francisco, CA 94121, United States; Department of Biochemistry & Biophysics, University of California, San Francisco, CA 94158, United States.

Gary Cecchini (G)

Molecular Biology Division, San Francisco VA Health Care System, San Francisco, CA 94121, United States; Department of Biochemistry & Biophysics, University of California, San Francisco, CA 94158, United States. Electronic address: gary.cecchini@ucsf.edu.

T M Iverson (TM)

Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, United States; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, United States; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, United States; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37232, United States. Electronic address: tina.iverson@vanderbilt.edu.

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Classifications MeSH