Bacterial Na(+)-ATP synthase has an undecameric rotor.
Détails
ID Serval
serval:BIB_BE88D1F8F40B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Bacterial Na(+)-ATP synthase has an undecameric rotor.
Périodique
EMBO reports
ISSN
1469-221X (Print)
ISSN-L
1469-221X
Statut éditorial
Publié
Date de publication
03/2001
Peer-reviewed
Oui
Volume
2
Numéro
3
Pages
229-233
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Résumé
Synthesis of adenosine triphosphate (ATP) by the F(1)F(0) ATP synthase involves a membrane-embedded rotary engine, the F(0) domain, which drives the extra-membranous catalytic F(1) domain. The F(0) domain consists of subunits a(1)b(2) and a cylindrical rotor assembled from 9-14 alpha-helical hairpin-shaped c-subunits. According to structural analyses, rotors contain 10 c-subunits in yeast and 14 in chloroplast ATP synthases. We determined the rotor stoichiometry of Ilyobacter tartaricus ATP synthase by atomic force microscopy and cryo-electron microscopy, and show the cylindrical sodium-driven rotor to comprise 11 c-subunits.
Mots-clé
Bacteria, Anaerobic/enzymology, Cryoelectron Microscopy, Crystallization, Microscopy, Atomic Force, Protein Structure, Tertiary, Protein Subunits, Proton-Translocating ATPases/chemistry, Proton-Translocating ATPases/metabolism, Proton-Translocating ATPases/ultrastructure, Rotation
Pubmed
Web of science
Open Access
Oui
Création de la notice
09/06/2023 15:04
Dernière modification de la notice
20/07/2023 5:57
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