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

Int J Med Microbiol

Interfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany; Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA. Electronic address:

Published: September 2019

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.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.ijmm.2019.151334DOI Listing

Publication Analysis

Top Keywords

enzyme complex
8
cell wall
8
unraveling mechanism
4
mechanism peptidoglycan
4
peptidoglycan amidation
4
amidation bifunctional
4
bifunctional enzyme
4
complex gatd/murt
4
gatd/murt comparative
4
comparative structural
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!