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