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How azide inhibits ATP hydrolysis by the F-ATPases

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Bowler, Matthew W., Montgomery, Martin G., Leslie, Andrew G. W., Walker, John E.·2006·Proceedings of the National Academy of Sciences

Abstract

In the structure of bovine F 1 -ATPase determined at 1.95-Å resolution with crystals grown in the presence of ADP, 5′-adenylyl-imidodiphosphate, and azide, the azide anion interacts with the β-phosphate of ADP and with residues in the ADP-binding catalytic subunit, β DP . It occupies a position between the catalytically essential amino acids, β-Lys-162 in the P loop and the “arginine finger” residue, α-Arg-373, similar to the site occupied by the γ-phosphate in the ATP-binding subunit, β TP . Its presence in the β DP -subunit tightens the binding of the side chains to the nucleotide, enhancing its affinity and thereby stabilizing the state with bound ADP. This mechanism of inhibition appears to be common to many other ATPases, including ABC transporters, SecA, and DNA topoisomerase IIα. It also explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding of ADP.

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Metadata

Authors
Bowler, M. W., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E.
Venue
Proceedings of the National Academy of Sciences
Published
2006-06-06
Volume
103
Issue
23
Pages
8646-8649
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2119010514
Cited by
244
References
2
FWCI
4.05
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: How azide inhibits ATP hydrolysis by the F-ATPases. https://app.cochat.ai/papers/10.1073/pnas.0602915103
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Bowler, M. W., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2006). How azide inhibits ATP hydrolysis by the F-ATPases. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0602915103

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