2jfw

Revision as of 19:09, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2jfw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jfw, resolution 22.Å" /> '''CRYSTAL STRUCTURE OF...)
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CRYSTAL STRUCTURE OF ENTEROCOCCUS FAECIUM GLUTAMATE RACEMASE IN COMPLEX WITH TARTRATE

File:2jfw.gif


2jfw, resolution 22.Å

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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 ... [(full description)]

About this StructureAbout this Structure

2JFW is a [Single protein] structure of sequence from [Enterococcus faecium] with TLA as [ligand]. Active as [[1]], with EC number [5.1.1.3]. 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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