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Mechanism of inhibition of DNA gyrase by quinolone antibacterials: a cooperative drug-DNA binding model

Shen, Linus L., Mitscher, Lester A., Sharma, Padam N., O'Donnell, T. J., Chu, Daniel W. T., Cooper, Curt S., Rosen, Terry, Pernet, Andre G.·1989·Biochemistry

Abstract

We have proposed a cooperative quinolone-DNA binding model for the inhibition of DNA gyrase. The essential feature of the model is that bound gyrase induces a specific quinolone binding site in the relaxed DNA substrate in the presence of ATP. The binding affinity and specificity are derived from two unique and equally important functional features: the specific conformation of the proposed single-stranded DNA pocket induced by the enzyme and the unique self-association phenomenon (from which the cooperativity is derived) of the drug molecules to fit the binding pocket with a high degree of flexibility. Supporting evidence for and implications of this model are provided.

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Metadata

Authors
Shen, L. L., Mitscher, L. A., Sharma, P. N., O'Donnell, T. J., Chu, D. W. T., Cooper, C. S., Rosen, T., & Pernet, A. G.
Venue
Biochemistry
Published
1989-05-02
Volume
28
Issue
9
Pages
3886-3894
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2052467184
Cited by
413
References
0
FWCI
5.58
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Mechanism of inhibition of DNA gyrase by quinolone antibacterials: a cooperative drug-DNA binding model. https://app.cochat.ai/papers/10.1021/bi00435a039
The paper
Shen, L. L., Mitscher, L. A., Sharma, P. N., O'Donnell, T. J., Chu, D. W. T., Cooper, C. S., Rosen, T., & Pernet, A. G. (1989). Mechanism of inhibition of DNA gyrase by quinolone antibacterials: a cooperative drug-DNA binding model. Biochemistry. https://doi.org/10.1021/bi00435a039

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.