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2ohg

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Revision as of 06:51, 22 August 2018

Structural Basis for Glutamte Racemase Inhibition

Structural highlights

2ohg is a 1 chain structure with sequence from Streptococcus pyogenes (serotype 1 / m1 gas). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1b73, 1zuw, 2oho, 2ohv
Gene:	murI (Streptococcus pyogenes (serotype 1 / M1 GAS))
Activity:	Glutamate racemase, with EC number 5.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MURI_STRP1] Provides the (R)-glutamate required for cell wall biosynthesis (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE. Structural basis for glutamate racemase inhibition. J Mol Biol. 2007 Sep 14;372(2):434-43. Epub 2007 May 10. PMID:17658548 doi:http://dx.doi.org/10.1016/j.jmb.2007.05.003

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ohg"

Categories: Glutamate racemase | Kim, E E | Isomerase | Racemase

@@ Line 1: / Line 1: @@
 ==Structural Basis for Glutamte Racemase Inhibition==
 <StructureSection load='2ohg' size='340' side='right' caption='[[2ohg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">murI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160490 Streptococcus pyogenes (serotype 1 / M1 GAS)])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ohg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ohg OCA], [http://pdbe.org/2ohg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ohg RCSB], [http://www.ebi.ac.uk/pdbsum/2ohg PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ohg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ohg OCA], [http://pdbe.org/2ohg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ohg RCSB], [http://www.ebi.ac.uk/pdbsum/2ohg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ohg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oh/2ohg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oh/2ohg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2ohg

From Proteopedia

Revision as of 06:51, 22 August 2018

Structural Basis for Glutamte Racemase Inhibition

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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