5maa: Difference between revisions
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<StructureSection load='5maa' size='340' side='right'caption='[[5maa]], [[Resolution|resolution]] 1.69Å' scene=''> | <StructureSection load='5maa' size='340' side='right'caption='[[5maa]], [[Resolution|resolution]] 1.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5maa]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5maa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurospirillum_multivorans_DSM_12446 Sulfurospirillum multivorans DSM 12446]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MAA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3R:3-BROMOPHENOL'>B3R</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OBL:5-Methoxybenzimidazolyl-norcobamide'>OBL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.686Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3R:3-BROMOPHENOL'>B3R</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OBL:5-Methoxybenzimidazolyl-norcobamide'>OBL</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5maa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5maa OCA], [https://pdbe.org/5maa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5maa RCSB], [https://www.ebi.ac.uk/pdbsum/5maa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5maa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sulfurospirillum multivorans | [[Category: Sulfurospirillum multivorans DSM 12446]] | ||
[[Category: Bommer | [[Category: Bommer M]] | ||
[[Category: Diekert | [[Category: Diekert G]] | ||
[[Category: Dobbek | [[Category: Dobbek H]] | ||
[[Category: Hagen | [[Category: Hagen WR]] | ||
[[Category: Kunze | [[Category: Kunze C]] | ||
[[Category: Schubert | [[Category: Schubert T]] | ||
[[Category: Uksa | [[Category: Uksa M]] | ||
Latest revision as of 21:34, 1 November 2023
PCE reductive dehalogenase from S. multivorans in complex with 3-bromophenolPCE reductive dehalogenase from S. multivorans in complex with 3-bromophenol
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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