Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

TitleStructure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
Publication TypeJournal Article
Year of Publication1994
AuthorsAbrahams, JP, Leslie, AG, Lutter, R, Walker, JE
JournalNature
Volume370
Issue6491
Pagination621-8
Date Published1994 Aug 25
ISSN0028-0836
KeywordsAmino Acid Sequence, Animals, Binding Sites, Catalysis, Cattle, Computer Graphics, Crystallography, X-Ray, Mitochondria, Heart, Models, Molecular, Molecular Sequence Data, Nucleotides, Protein Conformation, Proton-Translocating ATPases
Abstract

In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.

DOI10.1038/370621a0
Alternate JournalNature
Citation Key10.1038/370621a0
PubMed ID8065448