2jfn | pdb_00002jfn

CRYSTAL STRUCTURE OF ESCHERICHIA COLI GLUTAMATE RACEMASE IN COMPLEX WITH L-GLUTAMATE AND ACTIVATOR UDP-MURNAC-ALA

spinqualitylabelsall models 2jfn, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jfn is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLU, UMA Related: 2jfo, 2jfp, 2jfq, 2jfu Activity: Glutamate racemase, with EC number 5.1.1.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MURI_ECOLI] Provides the (R)-glutamate required for cell wall biosynthesis. 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 Glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and has therefore been considered as a target for antibacterial drug discovery. We characterized the glutamate racemases of several pathogenic bacteria using structural and biochemical approaches. Here we describe three distinct mechanisms of regulation for the family of glutamate racemases: allosteric activation by metabolic precursors, kinetic regulation through substrate inhibition, and D-glutamate recycling using a d-amino acid transaminase. In a search for selective inhibitors, we identified a series of uncompetitive inhibitors specifically targeting Helicobacter pylori glutamate racemase that bind to a cryptic allosteric site, and used these inhibitors to probe the mechanistic and dynamic features of the enzyme. These structural, kinetic and mutational studies provide insight into the physiological regulation of these essential enzymes and provide a basis for designing narrow-spectrum antimicrobial agents. Exploitation of structural and regulatory diversity in glutamate racemases.,Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL Nature. 2007 Jun 14;447(7146):817-22. PMID:17568739 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutamate racemase

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