View source for 6xck


==Crystal structure of C-As lyase with mutation K105E==
<StructureSection load='6xck' size='340' side='right'caption='[[6xck]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata_DSM_43183 Thermomonospora curvata DSM 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XCK 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]] 1.62&#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=6xck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xck OCA], [https://pdbe.org/6xck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xck RCSB], [https://www.ebi.ac.uk/pdbsum/6xck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xck ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D1A230_THECD D1A230_THECD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Organoarsenicals such as monosodium methylarsenate (MSMA or MAs(V)) and roxarsone (4-hydroxyl-3-nitrophenylarsenate or Rox(V)) have been extensively used as herbicides and growth enhancers for poultry, respectively. Degradation of organoarsenicals to inorganic arsenite (As(III)) contaminates crops and drinking water. One such process is catalyzed by the bacterial enzyme ArsI, whose gene is found in many soil bacteria. ArsI is a non-heme ferrous iron (Fe(II))-dependent dioxygenase that catalyzes oxygen-dependent cleavage of the carbonarsenic (C-As) bond in trivalent organoarsenicals, degrading them to inorganic As(III). From previous crystal structures of ArsI, we predicted that a loop-gating mechanism controls the catalytic reaction. Understanding the catalytic mechanism of ArsI requires knowledge of the mechanisms of substrate binding and activation of dioxygen. Here we report new ArsI structures with bound Rox(III) and mutant enzymes with alteration of active site residues. Our results elucidate steps in the catalytic cycle of this novel dioxygenase and enhance understanding of the recycling of environmental organoarsenicals.

The ArsI C-As lyase: Elucidating the catalytic mechanism of degradation of organoarsenicals.,Nadar VS, Kandavelu P, Sankaran B, Rosen BP, Yoshinaga M J Inorg Biochem. 2022 Jul;232:111836. doi: 10.1016/j.jinorgbio.2022.111836. Epub , 2022 Apr 20. PMID:35487149<ref>PMID:35487149</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xck" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomonospora curvata DSM 43183]]
[[Category: Kandavelu P]]
[[Category: Rosen BP]]
[[Category: Sankaran B]]
[[Category: Venkadesh S]]
[[Category: Yoshinaga M]]