5ma2: Difference between revisions
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==PCE reductive dehalogenase from S. multivorans in complex with 4-iodophenol== | ==PCE reductive dehalogenase from S. multivorans in complex with 4-iodophenol== | ||
<StructureSection load='5ma2' size='340' side='right' caption='[[5ma2]], [[Resolution|resolution]] 1.88Å' scene=''> | <StructureSection load='5ma2' size='340' side='right'caption='[[5ma2]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ma2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfurospirillum_multivorans Sulfurospirillum multivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MA2 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5ma2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfurospirillum_multivorans Sulfurospirillum multivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MA2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MA2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=BVQ:NORPSEUDO-B12'>BVQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=IOL:4-IODOPHENOL'>IOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=IOL:4-IODOPHENOL'>IOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5m2g|5m2g]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5m2g|5m2g]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ma2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ma2 OCA], [http://pdbe.org/5ma2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ma2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ma2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ma2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ma2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ma2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sulfurospirillum multivorans]] | [[Category: Sulfurospirillum multivorans]] | ||
[[Category: Bommer, M]] | [[Category: Bommer, M]] | ||
Revision as of 10:13, 19 August 2020
PCE reductive dehalogenase from S. multivorans in complex with 4-iodophenolPCE reductive dehalogenase from S. multivorans in complex with 4-iodophenol
Structural highlights
Publication Abstract from PubMedThe capacity of metal-containing porphyrinoids to mediate reductive dehalogenation is implemented in cobamide-containing reductive dehalogenases (RDases), which serve as terminal reductases in organohalide-respiring microbes. RDases allow for the exploitation of halogenated compounds as electron acceptors. Their reaction mechanism is under debate. Here we report on substrate-enzyme interactions in a tetrachloroethene RDase (PceA) that also converts aryl halides. The shape of PceA's highly apolar active site directs binding of bromophenols at some distance from the cobalt and with the hydroxyl substituent towards the metal. A close cobalt-substrate interaction is not observed by electron paramagnetic resonance spectroscopy. Nonetheless, a halogen substituent para to the hydroxyl group is reductively eliminated and the path of the leaving halide is traced in the structure. Based on these findings, an enzymatic mechanism relying on a long-range electron transfer is concluded, which is without parallel in vitamin B12-dependent biochemistry and represents an effective mode of RDase catalysis. Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer.,Kunze C, Bommer M, Hagen WR, Uksa M, Dobbek H, Schubert T, Diekert G Nat Commun. 2017 Jul 3;8:15858. doi: 10.1038/ncomms15858. PMID:28671181[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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