2ohg

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{{Seed}}
 
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[[Image:2ohg.png|left|200px]]
 
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==Structural Basis for Glutamte Racemase Inhibition==
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The line below this paragraph, containing "STRUCTURE_2ohg", creates the "Structure Box" on the page.
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<StructureSection load='2ohg' size='340' side='right'caption='[[2ohg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ohg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_M1_GAS Streptococcus pyogenes M1 GAS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OHG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ohg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ohg OCA], [https://pdbe.org/2ohg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ohg RCSB], [https://www.ebi.ac.uk/pdbsum/2ohg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ohg ProSAT]</span></td></tr>
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{{STRUCTURE_2ohg| PDB=2ohg | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MURI_STRP1 MURI_STRP1] Provides the (R)-glutamate required for cell wall biosynthesis (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oh/2ohg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ohg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structural Basis for Glutamte Racemase Inhibition===
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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<ref>PMID:17658548</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ohg" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17658548}}, adds the Publication Abstract to the page
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*[[Glutamate racemase 3D structures|Glutamate racemase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17658548 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17658548}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2OHG is a 1 chain 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].
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[[Category: Streptococcus pyogenes M1 GAS]]
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[[Category: Kim EE]]
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==Reference==
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<ref group="xtra">PMID:17658548</ref><references group="xtra"/>
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[[Category: Glutamate racemase]]
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[[Category: Streptococcus pyogenes]]
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[[Category: Kim, E E.]]
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[[Category: Isomerase]]
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[[Category: Racemase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 10:01:46 2009''
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Current revision

Structural Basis for Glutamte Racemase Inhibition

PDB ID 2ohg

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