In Crystallo Time-Resolved Interaction of the Clostridioides difficile CDD-1 enzyme with Avibactam Provides New Insights into the Catalytic Mechanism of Class D β-lactamases-Reference-Cited by-同舟云学术

In Crystallo Time-Resolved Interaction of the Clostridioides difficile CDD-1 enzyme with Avibactam Provides New Insights into the Catalytic Mechanism of Class D β-lactamases

Published:2021-04-28 Issue:6 Volume:7 Page:1765-1776
ISSN:2373-8227
Container-title:ACS Infectious Diseases
language:en
Short-container-title:ACS Infect. Dis.

Author:

Stewart Nichole K.¹,Toth Marta¹,Stasyuk Anastasiya²,Vakulenko Sergei B.¹,Smith Clyde A.²³^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States

2. Stanford Synchrotron Radiation Lightsource, Stanford University, Menlo Park, California 94025, United States

3. Department of Chemistry, Stanford University, Stanford, California 94305, United States

Funder

National Center for Research Resources

National Institute of Allergy and Infectious Diseases

Publisher

American Chemical Society (ACS)

Subject

Infectious Diseases

Link

https://pubs.acs.org/doi/pdf/10.1021/acsinfecdis.1c00094

Reference55 articles.

1. The structure of β-lactamases

2. Past and Present Perspectives on β-Lactamases

3. β-Lactam Resistance Mechanisms: Gram-Positive Bacteria andMycobacterium tuberculosis

4. A surface loop modulates activity of the Bacillus class D β-lactamases

5. Class D β-lactamases do exist in Gram-positive bacteria

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