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1b73

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(New page: 200px<br /><applet load="1b73" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b73, resolution 2.3&Aring;" /> '''GLUTAMATE RACEMASE FR...)
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[[Image:1b73.jpg|left|200px]]<br /><applet load="1b73" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b73, resolution 2.3&Aring;" />
 
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'''GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS'''<br />
 
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==Overview==
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==GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS==
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Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell, walls. The crystal structure of glutamate racemase from Aquifex, pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms, a dimer and each monomer consists of two alpha/beta fold domains, a unique, structure that has not been observed in other racemases or members of an, enolase superfamily. A substrate analog, D-glutamine, binds to the deep, pocket formed by conserved residues from two monomers. The structural and, mutational analyses allow us to propose a mechanism of metal, cofactor-independent glutamate racemase in which two cysteine residues are, involved in catalysis.
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<StructureSection load='1b73' size='340' side='right'caption='[[1b73]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b73]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_pyrophilus Aquifex pyrophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B73 FirstGlance]. <br>
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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]] 2.3&#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=1b73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b73 OCA], [https://pdbe.org/1b73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b73 RCSB], [https://www.ebi.ac.uk/pdbsum/1b73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b73 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MURI_AQUPY MURI_AQUPY] Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.
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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/b7/1b73_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=1b73 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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Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls. The crystal structure of glutamate racemase from Aquifex pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms a dimer and each monomer consists of two alpha/beta fold domains, a unique structure that has not been observed in other racemases or members of an enolase superfamily. A substrate analog, D-glutamine, binds to the deep pocket formed by conserved residues from two monomers. The structural and mutational analyses allow us to propose a mechanism of metal cofactor-independent glutamate racemase in which two cysteine residues are involved in catalysis.
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==About this Structure==
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Structure and mechanism of glutamate racemase from Aquifex pyrophilus.,Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y Nat Struct Biol. 1999 May;6(5):422-6. PMID:10331867<ref>PMID:10331867</ref>
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1B73 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_pyrophilus Aquifex pyrophilus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B73 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure and mechanism of glutamate racemase from Aquifex pyrophilus., Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y, Nat Struct Biol. 1999 May;6(5):422-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10331867 10331867]
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</div>
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[[Category: Aquifex pyrophilus]]
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<div class="pdbe-citations 1b73" style="background-color:#fffaf0;"></div>
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[[Category: Glutamate racemase]]
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[[Category: Single protein]]
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[[Category: Cho, C.S.]]
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[[Category: Cho, Y.]]
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[[Category: Hwang, K.Y.]]
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[[Category: Kim, S.S.]]
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[[Category: Yu, Y.G.]]
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[[Category: isomerase]]
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[[Category: racemase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:25:00 2007''
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==See Also==
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*[[Glutamate racemase 3D structures|Glutamate racemase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aquifex pyrophilus]]
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[[Category: Large Structures]]
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[[Category: Cho CS]]
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[[Category: Cho Y]]
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[[Category: Hwang KY]]
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[[Category: Kim SS]]
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[[Category: Yu YG]]

Current revision

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

PDB ID 1b73

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