2ohg
From Proteopedia
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| - | [[Image:2ohg.jpg|left|200px]] | + | [[Image:2ohg.jpg|left|200px]] |
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| - | '''Structural Basis for Glutamte Racemase Inhibition''' | + | {{Structure |
| + | |PDB= 2ohg |SIZE=350|CAPTION= <scene name='initialview01'>2ohg</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= murI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1314 Streptococcus pyogenes]) | ||
| + | }} | ||
| + | |||
| + | '''Structural Basis for Glutamte Racemase Inhibition''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OHG is a [ | + | 2OHG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OHG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17658548 17658548] |
[[Category: Glutamate racemase]] | [[Category: Glutamate racemase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: racemase]] | [[Category: racemase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:59:46 2008'' |
Revision as of 15:59, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | murI (Streptococcus pyogenes) | ||||||
| Activity: | Glutamate racemase, with EC number 5.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural Basis for Glutamte Racemase Inhibition
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
2OHG is a Single protein structure of sequence from Streptococcus pyogenes. 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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