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| [[Image:2jfx.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2jfx| PDB=2jfx | SCENE= }} | | {{STRUCTURE_2jfx| PDB=2jfx | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF HELICOBACTER PYLORI GLUTAMATE RACEMASE IN COMPLEX WITH D-GLUTAMATE'''
| | ===CRYSTAL STRUCTURE OF HELICOBACTER PYLORI GLUTAMATE RACEMASE IN COMPLEX WITH D-GLUTAMATE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17568739}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17568739 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17568739}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Peptidoglycan biosynthesis]] | | [[Category: Peptidoglycan biosynthesis]] |
| [[Category: Peptidoglycan synthesis]] | | [[Category: Peptidoglycan synthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:51:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:02:54 2008'' |