Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.
Journal Article (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 Mg(2+) 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, D-Y; Guan, Z; Hong, J; Zhou, P; Lee, S-Y
Published Date
- August 30, 2013
Published In
Volume / Issue
- 341 / 6149
Start / End Page
- 1012 - 1016
PubMed ID
- 23990562
Pubmed Central ID
- 23990562
Electronic International Standard Serial Number (EISSN)
- 1095-9203
Digital Object Identifier (DOI)
- 10.1126/science.1236501
Language
- eng
Conference Location
- United States