View source for 1b73


==GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS==
<StructureSection load='1b73' size='340' side='right'caption='[[1b73]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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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== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b7/1b73_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Glutamate racemase 3D structures|Glutamate racemase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex pyrophilus]]
[[Category: Large Structures]]
[[Category: Cho CS]]
[[Category: Cho Y]]
[[Category: Hwang KY]]
[[Category: Kim SS]]
[[Category: Yu YG]]