Structure of the mitochondrial ATP synthase by electron cryomicroscopy.

TitleStructure of the mitochondrial ATP synthase by electron cryomicroscopy.
Publication TypeJournal Article
Year of Publication2003
AuthorsRubinstein, JL, Walker, JE, Henderson, R
JournalEMBO J
Volume22
Issue23
Pagination6182-92
Date Published2003 Dec 01
ISSN0261-4189
KeywordsAnimals, Cattle, Cryoelectron Microscopy, Image Processing, Computer-Assisted, Mitochondria, Heart, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Protein Conformation, Protein Structure, Secondary, Rotation
Abstract

We have determined the structure of intact ATP synthase from bovine heart mitochondria by electron cryomicroscopy of single particles. Docking of an atomic model of the F1-c10 subcomplex into a major segment of the map has allowed the 32 A resolution density to be interpreted as the F1-ATPase, a central and a peripheral stalk and an FO membrane region that is composed of two domains. One domain of FO corresponds to the ring of c-subunits, and the other probably contains the a-subunit, the transmembrane portion of the b-subunit and the remaining integral membrane proteins of FO. The peripheral stalk wraps around the molecule and connects the apex of F1 to the second domain of FO. The interaction of the peripheral stalk with F1-c10 implies that it binds to a non-catalytic alpha-beta interface in F1 and its inclination where it is not attached to F1 suggests that it has a flexible region that can serve as a stator during both ATP synthesis and ATP hydrolysis.

DOI10.1093/emboj/cdg608
Alternate JournalEMBO J.
Citation Key10.1093/emboj/cdg608
PubMed ID14633978
PubMed Central IDPMC291849