Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.

TitleNovel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.
Publication TypeJournal Article
Year of Publication2006
AuthorsKabaleeswaran, V, Puri, N, Walker, JE, Leslie, AGW, Mueller, DM
JournalEMBO J
Volume25
Issue22
Pagination5433-42
Date Published2006 Nov 15
ISSN0261-4189
KeywordsAdenosine Diphosphate, Animals, Catalysis, Catalytic Domain, Cattle, Mitochondria, Models, Molecular, Protein Conformation, Protein Folding, Proton-Translocating ATPases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Abstract

The crystal structure of yeast mitochondrial F(1) ATPase contains three independent copies of the complex, two of which have similar conformations while the third differs in the position of the central stalk relative to the alpha(3)beta(3) sub-assembly. All three copies display very similar asymmetric features to those observed for the bovine enzyme, but the yeast F(1) ATPase structures provide novel information. In particular, the active site that binds ADP in bovine F(1) ATPase has an ATP analog bound and therefore this structure does not represent the ADP-inhibited form. In addition, one of the complexes binds phosphate in the nucleotide-free catalytic site, and comparison with other structures provides a picture of the movement of the phosphate group during initial binding and subsequent catalysis. The shifts in position of the central stalk between two of the three copies of yeast F(1) ATPase and when these structures are compared to those of the bovine enzyme give new insight into the conformational changes that take place during rotational catalysis.

DOI10.1038/sj.emboj.7601410
Alternate JournalEMBO J.
Citation Key10.1038/sj.emboj.7601410
PubMed ID17082766
PubMed Central IDPMC1636620
Grant ListR01 GM066223 / GM / NIGMS NIH HHS / United States
R01-GM066223 / GM / NIGMS NIH HHS / United States
F06 TW002379 / TW / FIC NIH HHS / United States
R01 GM067091 / GM / NIGMS NIH HHS / United States
1F06TW002379 / TW / FIC NIH HHS / United States
MC_U105184325 / / Medical Research Council / United Kingdom
R01-GM067091 / GM / NIGMS NIH HHS / United States
MC_U105663150 / / Medical Research Council / United Kingdom