Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.

TitleStructure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.
Publication TypeJournal Article
Year of Publication2011
AuthorsCingolani, G, Duncan, TM
JournalNat Struct Mol Biol
Volume18
Issue6
Pagination701-7
Date Published2011 Jun
ISSN1545-9985
KeywordsATP Synthetase Complexes, Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Protein Conformation, Protein Structure, Quaternary
Abstract

ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, autoinhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit ɛ adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme and engages both rotor and stator subunits in extensive contacts that are incompatible with functional rotation. As a result, the three catalytic subunits are stabilized in a set of conformations and rotational positions distinct from previous F(1) structures.

DOI10.1038/nsmb.2058
Alternate JournalNat. Struct. Mol. Biol.
Citation Key10.1038/nsmb.2058
PubMed ID21602818
PubMed Central IDPMC3109198
Grant ListR01 GM083088 / GM / NIGMS NIH HHS / United States
R01 GM083088-02 / GM / NIGMS NIH HHS / United States
R01GM083088 / GM / NIGMS NIH HHS / United States