1b74

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[[Image:1b74.png|left|200px]]
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==GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS==
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<StructureSection load='1b74' size='340' side='right' caption='[[1b74]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b74]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_pyrophilus Aquifex pyrophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B74 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGN:D-GLUTAMINE'>DGN</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b73|1b73]]</td></tr>
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<tr><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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b74 RCSB], [http://www.ebi.ac.uk/pdbsum/1b74 PDBsum]</span></td></tr>
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<table>
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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/b7/1b74_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/chain_selection.php?pdb_ID=2ata 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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{{STRUCTURE_1b74| PDB=1b74 | SCENE= }}
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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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===GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS===
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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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{{ABSTRACT_PUBMED_10331867}}
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==See Also==
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*[[Glutamate racemase|Glutamate racemase]]
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==About this Structure==
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== References ==
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[[1b74]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_pyrophilus Aquifex pyrophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B74 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:010331867</ref><references group="xtra"/>
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[[Category: Aquifex pyrophilus]]
[[Category: Aquifex pyrophilus]]
[[Category: Glutamate racemase]]
[[Category: Glutamate racemase]]

Revision as of 03:16, 7 August 2014

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

1b74, resolution 2.30Å

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