2oho
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(New page: 200px<br /><applet load="2oho" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oho, resolution 2.25Å" /> '''Structural Basis for...)
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Revision as of 11:26, 23 January 2008
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Structural Basis for Glutamate Racemase Inhibitor
Overview
d-Glutamic acid is a required biosynthetic building block for, peptidoglycan, and the enzyme glutamate racemase (GluR) catalyzes the, inter-conversion of D and L-glutamate enantiomers. Therefore, GluR is, considered as an attractive target for the design of new antibacterial, drugs. Here, we report the crystal structures of GluR from Streptococcus, pyogenes in both inhibitor-free and inhibitor-bound forms. The inhibitor, free GluR crystallized in two different forms, which diffracted to 2.25 A, and 2.5 A resolution, while the inhibitor-bound crystal diffracted to 2.5, A resolution. GluR is composed of two domains of alpha/beta protein that, are related by pseudo-2-fold symmetry and the active site is located at, the domain interface. The inhibitor, gamma-2-naphthylmethyl-d-glutamate, which was reported earlier as a novel potent competitive inhibitor, makes, several hydrogen bonds with protein atoms, and the naphthyl moiety is, located in the hydrophobic pocket. The inhibitor binding induces a, disorder in one of the loops near the active site. In both crystal forms, GluR exists as a dimer and the interactions seen at the dimer interface, are almost identical. This agrees well with the results from gel, filtration and dynamic light-scattering studies.
About this Structure
2OHO is a Single protein structure of sequence from Streptococcus pyogenes with as ligand. Active as Glutamate racemase, with EC number 5.1.1.3 Full crystallographic information is available from OCA.
Reference
Structural basis for glutamate racemase inhibition., Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE, J Mol Biol. 2007 Sep 14;372(2):434-43. Epub 2007 May 10. PMID:17658548
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