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Unraveling the mechanism of peptidoglycan amidation by the bifunctional enzyme complex GatD/MurT: A comparative structural approach
Authors:Erik R. Nöldeke  Thilo Stehle
Affiliation:1. Interfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany;2. Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA
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.
Keywords:Corresponding author.  Crystal structure  bacterial cell wall protein
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