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

Int J Med Microbiol. 2019 Sep;309(6):151334. doi: 10.1016/j.ijmm.2019.151334. Epub 2019 Jul 18.

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: Crystal structure; bacterial cell wall protein.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Cell Wall / enzymology
  • Cell Wall / metabolism
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / metabolism*
  • Peptidoglycan / chemistry
  • Peptidoglycan / metabolism*
  • Protein Domains
  • Staphylococcus / enzymology
  • Staphylococcus / metabolism
  • Structure-Activity Relationship
  • Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives
  • Uridine Diphosphate N-Acetylmuramic Acid / metabolism

Substances

  • Bacterial Proteins
  • Multienzyme Complexes
  • Peptidoglycan
  • Uridine Diphosphate N-Acetylmuramic Acid
  • muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol