View source for 4rdz


==Crystal structure of VmoLac in P64 space group==
<StructureSection load='4rdz' size='340' side='right'caption='[[4rdz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rdz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vulcanisaeta_moutnovskia_768-28 Vulcanisaeta moutnovskia 768-28]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RDZ 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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=4rdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rdz OCA], [https://pdbe.org/4rdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rdz RCSB], [https://www.ebi.ac.uk/pdbsum/4rdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rdz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F0QXN6_VULM7 F0QXN6_VULM7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A new representative of the Phosphotriesterase-Like Lactonases (PLLs) family from the hyperthermophilic crenarchaeon Vulcanisaeta moutnovskia has been characterized and crystallized. VmoLac is a native, proficient lactonase with promiscuous, low phosphotriesterase activity. VmoLac therefore represents an interesting candidate for engineering studies, with the aim of developing an efficient bacterial quorum-quenching agent. Here, we provide an extensive biochemical and kinetic characterization of VmoLac and describe the X-ray structures of the enzyme bound to a fatty acid and to its cognate substrate 3-oxo-C10 AHL (Acyl-Homoserine Lactone). The structures highlight possible structural determinants that may be involved in its extreme thermal stability (Tm = 128 degrees C). Moreover, the structure reveals that the substrate binding mode of VmoLac significantly differs from those of its close homologues, possibly explaining the substrate specificity of the enzyme. Finally, we describe the specific interactions between the enzyme and its substrate, and discuss the possible lactone hydrolysis mechanism of VmoLac.

Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.,Hiblot J, Bzdrenga J, Champion C, Chabriere E, Elias M Sci Rep. 2015 Feb 11;5:8372. doi: 10.1038/srep08372. PMID:25670483<ref>PMID:25670483</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rdz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vulcanisaeta moutnovskia 768-28]]
[[Category: Bzdrenga J]]
[[Category: Chabriere E]]
[[Category: Champion C]]
[[Category: Elias M]]
[[Category: Gonzalez D]]
[[Category: Gotthard G]]
[[Category: Hiblot J]]