4j72
Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferaseCrystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase
Structural highlights
FunctionMRAY_AQUAE First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (By similarity). Publication Abstract from PubMedMraY (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 A 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. Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.,Chung BC, Zhao J, Gillespie RA, Kwon DY, Guan Z, Hong J, Zhou P, Lee SY Science. 2013 Aug 30;341(6149):1012-6. doi: 10.1126/science.1236501. PMID:23990562[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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