Literature DB >> 31383542

Unraveling the mechanism of peptidoglycan amidation by the bifunctional enzyme complex GatD/MurT: A comparative structural approach.

Erik R Nöldeke1, Thilo Stehle2.   

Abstract

The bacterial cell wall provides structural integrity to the cell and protects the cell from internal pressure and the external environment. During the course of the twelve-year funding period of the Collaborative Research Center 766, our work has focused on conducting structure-function studies of enzymes that modify (synthesize or cleave) cell wall components of a range of bacteria including Staphylococcus aureus, Staphylococcus epidermidis, and Nostoc punctiforme. Several of our structures represent promising targets for interference. In this review, we highlight a recent structure-function analysis of an enzyme complex that is responsible for the amidation of Lipid II, a peptidoglycan precursor, in S. aureus.
Copyright © 2019 Elsevier GmbH. All rights reserved.

Entities:  

Keywords:  Crystal structure; bacterial cell wall protein

Year:  2019        PMID: 31383542     DOI: 10.1016/j.ijmm.2019.151334

Source DB:  PubMed          Journal:  Int J Med Microbiol        ISSN: 1438-4221            Impact factor:   3.473


  2 in total

1.  CroR Regulates Expression of pbp4(5) to Promote Cephalosporin Resistance in Enterococcus faecalis.

Authors:  Sarah B Timmler; Stephanie L Kellogg; Samantha N Atkinson; Jaime L Little; Dušanka Djorić; Christopher J Kristich
Journal:  mBio       Date:  2022-08-01       Impact factor: 7.786

2.  Characterization of the MurT/GatD complex in Mycobacterium tuberculosis towards validating a novel anti-tubercular drug target.

Authors:  Arundhati Maitra; Syamasundari Nukala; Rachael Dickman; Liam T Martin; Tulika Munshi; Antima Gupta; Adrian J Shepherd; Kristine B Arnvig; Alethea B Tabor; Nicholas H Keep; Sanjib Bhakta
Journal:  JAC Antimicrob Resist       Date:  2021-03-16
  2 in total

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