4ur1: Difference between revisions
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The | ==Crystal structure of the PCE reductive dehalogenase from S. multivorans in complex with dibromoethene== | ||
<StructureSection load='4ur1' size='340' side='right'caption='[[4ur1]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ur1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurospirillum_multivorans Sulfurospirillum multivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UR1 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]] 1.649Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=BVQ:NORPSEUDO-B12'>BVQ</scene>, <scene name='pdbligand=CB0:CIS-DIBROMOETHENE'>CB0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=4ur1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ur1 OCA], [https://pdbe.org/4ur1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ur1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ur1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ur1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Organohalide-respiring microorganisms can use a variety of persistent pollutants including trichloroethene (TCE) as terminal electron acceptors. The final two-electron transfer step in organohalide respiration is catalyzed by reductive dehalogenases. Here we report the x-ray crystal structure of PceA, an archetypal dehalogenase from Sulfurospirillum multivorans, as well as structures of PceA in complex with TCE and product analogs. The active site harbors a deeply buried norpseudo-B12 cofactor within a nitroreductase fold, also found in a mammalian B12 chaperone. The structures of PceA reveal how a cobalamin supports a reductive haloelimination exploiting a conserved B12-binding scaffold capped by a highly variable substrate-capturing region. | |||
Structural basis for organohalide respiration.,Bommer M, Kunze C, Fesseler J, Schubert T, Diekert G, Dobbek H Science. 2014 Oct 2. pii: 1258118. PMID:25278505<ref>PMID:25278505</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ur1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfurospirillum multivorans]] | |||
[[Category: Bommer M]] | |||
[[Category: Diekert G]] | |||
[[Category: Dobbek H]] | |||
[[Category: Fesseler J]] | |||
[[Category: Kunze C]] | |||
[[Category: Schubert T]] | |||
Latest revision as of 14:22, 9 May 2024
Crystal structure of the PCE reductive dehalogenase from S. multivorans in complex with dibromoetheneCrystal structure of the PCE reductive dehalogenase from S. multivorans in complex with dibromoethene
Structural highlights
Publication Abstract from PubMedOrganohalide-respiring microorganisms can use a variety of persistent pollutants including trichloroethene (TCE) as terminal electron acceptors. The final two-electron transfer step in organohalide respiration is catalyzed by reductive dehalogenases. Here we report the x-ray crystal structure of PceA, an archetypal dehalogenase from Sulfurospirillum multivorans, as well as structures of PceA in complex with TCE and product analogs. The active site harbors a deeply buried norpseudo-B12 cofactor within a nitroreductase fold, also found in a mammalian B12 chaperone. The structures of PceA reveal how a cobalamin supports a reductive haloelimination exploiting a conserved B12-binding scaffold capped by a highly variable substrate-capturing region. Structural basis for organohalide respiration.,Bommer M, Kunze C, Fesseler J, Schubert T, Diekert G, Dobbek H Science. 2014 Oct 2. pii: 1258118. PMID:25278505[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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