Structural model of F 1 –ATPase and the implications for rotary catalysis-Reference-Cited by-同舟云学术

Structural model of F 1 –ATPase and the implications for rotary catalysis

Published:2000-04-29 Issue:1396 Volume:355 Page:465-471
ISSN:0962-8436
Container-title:Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
language:en
Short-container-title:Phil. Trans. R. Soc. Lond. B

Author:

Leslie A. G. W.¹,Walker J. E.²

Affiliation:

1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

2. MRC Dunn Human Nutrition Unit, Hills Road, Cambridge, CB2 2XY, UK

Abstract

The crystal structure of bovine mitochondrial F 1 –ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalytic sites. Furthermore, the structure also suggests that catalysis is accompanied by a physical rotation of the centrally placed γ–subunit relative to the approximately spherical α 3 β 3 sub–assembly.

Publisher

The Royal Society

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology

Link

https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.2000.0588

Reference26 articles.

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2. Abrahams J. P. Buchanan S. K. Van Raaij M. J. Fearnley I. M. Leslie A. G. W. & Walker J. E. 1996 The structure of bovine F 1 -ATPase complexed with the peptide antibiotic efrapeptin. Proc. Natl Acad. Sci. USA 93 9420^9424.

3. The g subunit of the Escherichia coli F1- ATPase can be cross-linked near the glycine-rich loop region of a b subunit when ADP + Mg2+ occupies catalytic sites but not when ATP + Mg2+ is bound;Aggeler R.;J. Biol. Chem.,1993

4. Spatial precision of a catalytic carboxylate of F1-ATPase β subunit probed by introducing different carboxylate-containing side chains

5. Bianchet M. A. Hullihen J. Petersen P. L. & Amzel L. M. 1998 The 2.8-Ð structure of rat liver F 1 -ATPase: con¢guration of a critical intermediate in ATP synthesis/hydrolysis. Proc. Natl Acad. Sci. USA 95 11065^11 070.

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