View source for 5vej


==High resolution crystal structure of a fluoride-inhibited organo-phosphate-degrading metallohydrolase==
<StructureSection load='5vej' size='340' side='right'caption='[[5vej]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VEJ 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]] 1.301&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></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=5vej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vej OCA], [https://pdbe.org/5vej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vej RCSB], [https://www.ebi.ac.uk/pdbsum/5vej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vej ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93LD7_RHIRD Q93LD7_RHIRD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metal ion-dependent, organophosphate-degrading enzymes (OP hydrolases) have received increasing attention due to their ability to degrade and thus detoxify commonly used pesticides and nerve agents such as sarin and VX. These enzymes thus garner strong potential as bioremediators. The OP hydrolase from Agrobacterium radiobacter (OpdA) is one of the most efficient members of this group of enzymes. Previous studies have indicated that the choice of the hydrolysis-initiating nucleophile may depend on the pH of the reaction, with a metal ion-bridging hydroxide being preferred at lower pH (i.e. pH&lt;/=8.5), and a terminally coordinated hydroxide at higher pH (i.e. pH&gt;9.0). Furthermore, fluoride was shown to be a potent inhibitor of the reaction, but only at low pH. Here, the crystal structure (1.3A, pH6) of OpdA in presence of fluoride is described. While the first coordination sphere in the active site displays minimal changes in the presence of fluoride, the hydrogen bonding network that connects the dimetallic metal center to the substrate binding pocket is disrupted. Thus, the structure of fluoride-inhibited OpdA demonstrates the significance of this hydrogen bond network in controlling the mechanism and function of this enzyme.

High resolution crystal structure of a fluoride-inhibited organophosphate-degrading metallohydrolase.,Selleck C, Guddat LW, Ollis DL, Schenk G, Pedroso MM J Inorg Biochem. 2017 Jun 27. pii: S0162-0134(17)30221-0. doi:, 10.1016/j.jinorgbio.2017.06.013. PMID:28673485<ref>PMID:28673485</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vej" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Agrobacterium tumefaciens]]
[[Category: Large Structures]]
[[Category: Selleck C]]