1q3g | pdb_00001q3g

MurA (Asp305Ala) liganded with tetrahedral reaction intermediate

spinqualitylabelsall models 1q3g, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1q3g is a 16 chain structure with sequence from "aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, UDA NonStd Res: IAS Related: 1naw, 1uae, 1a2n, 1eyn, 1ejc, 1ejd, 1q36 Gene: MURA ("Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923) Activity: UDP-N-acetylglucosamine 1-carboxyvinyltransferase, with EC number 2.5.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MURA_ENTCC] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) constitute the small enzyme family of enolpyruvyl transferases, which catalyze the chemically unusual reaction of enolpyruvyl transfer. MurA catalyzes the first step in the biosynthesis of the bacterial cell wall; AroA is the sixth enzyme of the shikimate pathway leading to the synthesis of aromatic compounds in numerous microorganisms and plants. Because both metabolic pathways are absent from mammals but essential for the growth of microorganisms, MurA and AroA are attractive targets for the development of novel antimicrobial drugs. We have determined the x-ray structures of the D305A mutant of Enterobacter cloacae MurA and the D313A mutant of Escherichia coli AroA, both of which crystallized in the presence of their substrates. The structures depict the tetrahedral reaction intermediate states of the enzymes and prove that, without the aspartate side chain, the overall addition-elimination reaction in both enzymes is halted after the addition step. The presented structures lead to a new view of the catalytic mechanism and, moreover, provide an ideal starting point for the rational design of potent inhibitors of MurA and AroA. A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states.,Eschenburg S, Kabsch W, Healy ML, Schonbrunn E J Biol Chem. 2003 Dec 5;278(49):49215-22. Epub 2003 Sep 16. PMID:13129913 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enoylpyruvate transferase 3D structures

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