Three-Dimensional Structure of AmpC β-Lactamase from Escherichia coli Bound to a Transition-State Analogue: Possible Implications for the Oxyanion Hypothesis and for Inhibitor Design-Reference-Cited by-同舟云学术

Three-Dimensional Structure of AmpC β-Lactamase from Escherichia coli Bound to a Transition-State Analogue: Possible Implications for the Oxyanion Hypothesis and for Inhibitor Design

Published:1998-10-28 Issue:46 Volume:37 Page:16082-16092
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Usher Ken C.¹,Blaszczak Larry C.¹,Weston G. Scott¹,Shoichet Brian K.¹,Remington S. James¹

Affiliation:

1. Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, Infectious Disease Research, Lilly Research Laboratories, Eli Lilly & Co., Lilly Corporate Center, Indianapolis, Indiana 46285, and Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, Illinois 60611-3008

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi981210f

Reference58 articles.

1. The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution

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