Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-08

AUTHORS

Jan Pieter Abrahams, Andrew G. W. Leslie, René Lutter, John E. Walker

ABSTRACT

In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution, the three catalytic β-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 α3β3 subassembly relative to an α-helical domain of the γ-subunit. More... »

PAGES

621-628

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/370621a0

DOI

http://dx.doi.org/10.1038/370621a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037493843

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8065448


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