5mau
From Proteopedia
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<StructureSection load='5mau' size='340' side='right' caption='[[5mau]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='5mau' size='340' side='right' caption='[[5mau]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5mau]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MAU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mau]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyap4 Cyap4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MAU FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cyan7425_1434 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=395961 CYAP4])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mau OCA], [http://pdbe.org/5mau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mau RCSB], [http://www.ebi.ac.uk/pdbsum/5mau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mau ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mau OCA], [http://pdbe.org/5mau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mau RCSB], [http://www.ebi.ac.uk/pdbsum/5mau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mau ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Although structure and steady-state kinetics of Clds have been elucidated, many questions remain (e.g., the mechanism of chlorite cleavage and the pH dependence of the reaction). Here, we present high-resolution X-ray crystal structures of a dimeric Cld at pH 6.5 and 8.5, its fluoride and isothiocyanate complexes and the neutron structure at pH 9.0 together with the pH dependence of the Fe(III)/Fe(II) couple, and the UV-vis and resonance Raman spectral features. We demonstrate that the distal Arg127 cannot act as proton acceptor and is fully ionized even at pH 9.0 ruling out its proposed role in dictating the pH dependence of chlorite degradation. Stopped-flow studies show that (i) Compound I and hypochlorite do not recombine and (ii) Compound II is the immediately formed redox intermediate that dominates during turnover. Homolytic cleavage of chlorite is proposed. | ||
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| + | Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies.,Schaffner I, Mlynek G, Flego N, Puhringer D, Libiseller-Egger J, Coates L, Hofbauer S, Bellei M, Furtmuller PG, Battistuzzi G, Smulevich G, Djinovic-Carugo K, Obinger C ACS Catal. 2017 Nov 3;7(11):7962-7976. doi: 10.1021/acscatal.7b01749. Epub 2017, Oct 13. PMID:29142780<ref>PMID:29142780</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5mau" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Cyap4]] | ||
[[Category: Djinovic-Carugo, K]] | [[Category: Djinovic-Carugo, K]] | ||
[[Category: Mlynek, G]] | [[Category: Mlynek, G]] | ||
Revision as of 06:57, 31 January 2018
Crystal structure of dimeric chlorite dismutase from Cyanothece sp. PCC7425 (pH 6.5)
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