Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 34, Issue -, Pages 989-992Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0340989
Keywords
ATPase synthase; aurovertin; catalytic domain; crystal structure; inhibitory site; mitochondrion
Categories
Funding
- Medical Research Council [MC_U105663150] Funding Source: Medline
- Medical Research Council [MC_U105663150] Funding Source: researchfish
- MRC [MC_U105663150] Funding Source: UKRI
Ask authors/readers for more resources
An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F-1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies. They are the catalytic site, and the binding sites for the antibiotics aurovertin and efrapeptin and for the natural inhibitor protein, IF1.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available