Download MendeleyCrystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.
Chung, B.C., Zhao, J., Gillespie, R.A., Kwon, D.Y., Guan, Z., Hong, J., Zhou, P., Lee, S.Y.(2013) Science 341: 1012-1016
- PubMed: 23990562
- DOI: https://doi.org/10.1126/science.1236501
- Primary Citation of Related Structures:
4J72 - PubMed Abstract:
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.
Organizational Affiliation:
Department of Biochemistry, Duke University Medical Center, 2 Genome Ct, Durham, NC 27710, USA.
