3svl
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structural basis of the improvement of ChrR - a multi-purpose enzyme== | |
- | + | <StructureSection load='3svl' size='340' side='right'caption='[[3svl]], [[Resolution|resolution]] 2.20Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3svl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SVL 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]] 2.2Å</td></tr> | |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=3svl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3svl OCA], [https://pdbe.org/3svl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3svl RCSB], [https://www.ebi.ac.uk/pdbsum/3svl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3svl ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CHRR_ECOLI CHRR_ECOLI] Involved in the protection against chromate toxicity. Catalyzes the transfer of three electrons to Cr(6+) producing Cr(3+) and one electron to molecular oxygen without producing the toxic Cr(5+) species and only producing a minimal amount of reactive oxygen species (ROS). It can also reduce quinones, potassium ferricyanide, 2,6-dichloroindophenol, V(5+), Mo(6+), methylene blue and cytochrome c. The quinone reductase activity may protect against oxidative stress by preventing redox cycling of quinones which would otherwise generate ROS and by maintaining a pool of reduced quinone in the cell that is able to quench ROS directly. It is able to use both NAD or NADP equally well.<ref>PMID:14766567</ref> <ref>PMID:16621832</ref> <ref>PMID:17088379</ref> <ref>PMID:22558308</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Escherichia coli K-12]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Berthomieu C]] | ||
+ | [[Category: Bremond N]] | ||
+ | [[Category: Eswaramoorthy S]] | ||
+ | [[Category: Hienerwadel R]] | ||
+ | [[Category: Matin AC]] | ||
+ | [[Category: Poulain S]] | ||
+ | [[Category: Sylvester MD]] | ||
+ | [[Category: Van Der Lelie D]] | ||
+ | [[Category: Zhang YB]] |
Current revision
Structural basis of the improvement of ChrR - a multi-purpose enzyme
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