Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis

Journal Article

MraY (phospho-MurNAc-pentapeptide translocase) is an integral membrane enzyme that catalyzes an essential step of bacterial cell wall biosynthesis: the transfer of the peptidoglycan precursor phospho-MurNAc-pentapeptide to the lipid carrier undecaprenyl phosphate. MraY has long been considered a promising target for the development of antibiotics, but the lack of a structure has hindered mechanistic understanding of this critical enzyme and the enzyme superfamily in general. The superfamily includes enzymes involved in bacterial lipopolysaccharide/teichoic acid formation and eukaryotic N-linked glycosylation, modifications that are central in many biological processes. We present the crystal structure of MraY from Aquifex aeolicus (MraYAA) at 3.3 Å resolution, which allows us to visualize the overall architecture, locate Mg2+ within the active site, and provide a structural basis of catalysis for this class of enzyme.

Full Text

Duke Authors

Cited Authors

  • Chung, BC; Zhao, J; Gillespie, RA; Kwon, DY; Guan, Z; Hong, J; Zhou, P; Lee, SY

Published Date

  • 2013

Published In

Volume / Issue

  • 341 / 6149

Start / End Page

  • 1012 - 1016

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1240985