4j72 | pdb_00004j72

Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase

spinqualitylabelsall models 4j72, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j72 is a 2 chain structure with sequence from Aquifex aeolicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MRAY_AQUAE First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (By similarity). Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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