1zuw

<StructureSection load='1zuw' size='340' side='right' caption='[[1zuw]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1zuw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZUW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">racE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=1zuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zuw OCA], [http://pdbe.org/1zuw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zuw RCSB], [http://www.ebi.ac.uk/pdbsum/1zuw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zuw ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MURI1_BACSU MURI1_BACSU]] Provides the (R)-glutamate required for cell wall biosynthesis (By similarity).

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== Publication Abstract from PubMed ==

D-glutamate is an essential building block of the peptidoglycan layer in bacterial cell walls and can be synthesized from L-glutamate by glutamate racemase (RacE). The structure of a complex of B. subtilis RacE with D-glutamate reveals that the glutamate is buried in a deep pocket, whose formation at the interface of the enzyme's two domains involves a large-scale conformational rearrangement. These domains are related by pseudo-2-fold symmetry, which superimposes the two catalytic cysteine residues, which are located at equivalent positions on either side of the alpha carbon of the substrate. The structural similarity of these two domains suggests that the racemase activity of RacE arose as a result of gene duplication. The structure of the complex is dramatically different from that proposed previously and provides new insights into the RacE mechanism and an explanation for the potency of a family of RacE inhibitors, which have been developed as novel antibiotics.

 

<div class="pdbe-citations 1zuw" style="background-color:#fffaf0;"></div>

== References ==

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Glutamate racemase]]

[[Category: Baker, P J]]

[[Category: Rice, D W]]

[[Category: Ruzheinikov, S N]]

[[Category: Sedelnikova, S E]]

[[Category: Taal, M A]]

[[Category: Peptidoglycan biosynthesis]]