The Unusual Binding Mode of Cnicin to the Antibacterial Target Enzyme MurA Revealed by X-ray Crystallography-Reference-Cited by-同舟云学术

The Unusual Binding Mode of Cnicin to the Antibacterial Target Enzyme MurA Revealed by X-ray Crystallography

Published:2008-08-01 Issue:16 Volume:51 Page:5143-5147
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Steinbach Anke¹,Scheidig Axel J.¹,Klein Christian D.¹

Affiliation:

1. Pharmazeutische Chemie, Universität Heidelberg, Im Neuenheimer Feld 364, D-69120 Heidelberg, Germany, Zoologisches Institut—Abteilung für Strukturbiologie, Christian-Albrechts-Universität zu Kiel, Am Botanischen Garten 1-9, 24098 Kiel, Germany

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm800609p

Reference28 articles.

1. Sesquiterpene lactones are potent and irreversible inhibitors of the antibacterial target enzyme MurA

2. Identification and Characterization of New Inhibitors of the Escherichia coli MurA Enzyme

3. THE MECHANISM OF ACTION OF FOSFOMYCIN (PHOSPHONOMYCIN)

4. Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis The EMBL accession number for the sequence in this paper is X96711.

5. Comparative X-ray analysis of the un-liganded fosfomycin-target MurA

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