2jfv: Difference between revisions
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|PDB= 2jfv |SIZE=350|CAPTION= <scene name='initialview01'>2jfv</scene>, resolution 1.8Å | |PDB= 2jfv |SIZE=350|CAPTION= <scene name='initialview01'>2jfv</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=AC1:Flc+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Flc+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=FLC:CITRATE ANION'>FLC</scene> | |LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate_racemase Glutamate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.3 5.1.1.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_racemase Glutamate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.3 5.1.1.3] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfv OCA], [http://www.ebi.ac.uk/pdbsum/2jfv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jfv RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lundqvist, T.]] | [[Category: Lundqvist, T.]] | ||
[[Category: glutamate racemase]] | [[Category: glutamate racemase]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: peptidoglycan biosynthesis]] | [[Category: peptidoglycan biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:57:43 2008'' | ||
Revision as of 03:57, 31 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Activity: | Glutamate racemase, with EC number 5.1.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ENTEROCOCCUS FAECIUM GLUTAMATE RACEMASE IN COMPLEX WITH CITRATE
OverviewOverview
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.
About this StructureAbout this Structure
2JFV is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.
ReferenceReference
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
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