期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 34, 期 -, 页码 989-992出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0340989
关键词
ATPase synthase; aurovertin; catalytic domain; crystal structure; inhibitory site; mitochondrion
资金
- Medical Research Council [MC_U105663150] Funding Source: Medline
- Medical Research Council [MC_U105663150] Funding Source: researchfish
- MRC [MC_U105663150] Funding Source: UKRI
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.
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