2JFN
Crystal structure of Escherichia coli glutamate racemase in complex with L- Glutamate and activator UDP-MurNAc-ala
Summary for 2JFN
| Entry DOI | 10.2210/pdb2jfn/pdb |
| Related | 2JFO 2JFP 2JFQ 2JFU |
| Descriptor | GLUTAMATE RACEMASE, GLUTAMIC ACID, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE, ... (4 entities in total) |
| Functional Keywords | cell wall, isomerase, cell shape, udp- murnac-ala, peptidoglycan biosynthesis, glutamate racemase, peptidoglycan synthesis |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 31931.49 |
| Authors | Lundqvist, T. (deposition date: 2007-02-03, release date: 2007-07-03, Last modification date: 2024-05-08) |
| Primary citation | Lundqvist, T.,Fisher, S.L.,Kern, G.,Folmer, R.H.A.,Xue, Y.,Newton, D.T.,Keating, T.A.,Alm, R.A.,De Jonge, B.L.M. Exploitation of Structural and Regulatory Diversity in Glutamate Racemases Nature, 447:817-, 2007 Cited by PubMed Abstract: 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. PubMed: 17568739DOI: 10.1038/NATURE05689 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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