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| | <StructureSection load='3svl' size='340' side='right'caption='[[3svl]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3svl' size='340' side='right'caption='[[3svl]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3svl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. 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> | + | <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='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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yieF, b3713, JW3691 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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> | | <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> | | </table> |
| | == Function == | | == 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>
| + | [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> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The Escherichia coli ChrR enzyme is an obligatory two-electron quinone reductase that has many applications, such as in chromate bioremediation. Its crystal structure, solved at 2.2 A resolution, shows that it belongs to the flavodoxin superfamily in which flavin mononucleotide (FMN) is firmly anchored to the protein. ChrR crystallized as a tetramer, and size exclusion chromatography showed that this is the oligomeric form that catalyzes chromate reduction. Within the tetramer, the dimers interact by a pair of two hydrogen bond networks, each involving Tyr128 and Glu146 of one dimer and Arg125 and Tyr85 of the other; the latter extends to one of the redox FMN cofactors. Changes in each of these amino acids enhanced chromate reductase activity of the enzyme, showing that this network is centrally involved in chromate reduction.
| + | |
| - | | + | |
| - | Crystal Structure of ChrR-A Quinone Reductase with the Capacity to Reduce Chromate.,Eswaramoorthy S, Poulain S, Hienerwadel R, Bremond N, Sylvester MD, Zhang YB, Berthomieu C, Van Der Lelie D, Matin A PLoS One. 2012;7(4):e36017. Epub 2012 Apr 27. PMID:22558308<ref>PMID:22558308</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3svl" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berthomieu, C]] | + | [[Category: Berthomieu C]] |
| - | [[Category: Bremond, N]] | + | [[Category: Bremond N]] |
| - | [[Category: Eswaramoorthy, S]] | + | [[Category: Eswaramoorthy S]] |
| - | [[Category: Hienerwadel, R]] | + | [[Category: Hienerwadel R]] |
| - | [[Category: Lelie, D Van Der]]
| + | [[Category: Matin AC]] |
| - | [[Category: Matin, A C]] | + | [[Category: Poulain S]] |
| - | [[Category: Poulain, S]] | + | [[Category: Sylvester MD]] |
| - | [[Category: Sylvester, M D]] | + | [[Category: Van Der Lelie D]] |
| - | [[Category: Zhang, Y B]] | + | [[Category: Zhang YB]] |
| - | [[Category: Chromate bioremediation]] | + | |
| - | [[Category: E. coli chrr enzyme]]
| + | |
| - | [[Category: Improved mutant enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tetramer role]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
References
- ↑ Ackerley DF, Gonzalez CF, Park CH, Blake R 2nd, Keyhan M, Matin A. Chromate-reducing properties of soluble flavoproteins from Pseudomonas putida and Escherichia coli. Appl Environ Microbiol. 2004 Feb;70(2):873-82. PMID:14766567
- ↑ Ackerley DF, Barak Y, Lynch SV, Curtin J, Matin A. Effect of chromate stress on Escherichia coli K-12. J Bacteriol. 2006 May;188(9):3371-81. PMID:16621832 doi:http://dx.doi.org/10.1128/JB.188.9.3371-3381.2006
- ↑ Barak Y, Ackerley DF, Dodge CJ, Banwari L, Alex C, Francis AJ, Matin A. Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolution. Appl Environ Microbiol. 2006 Nov;72(11):7074-82. PMID:17088379 doi:http://dx.doi.org/72/11/7074
- ↑ Eswaramoorthy S, Poulain S, Hienerwadel R, Bremond N, Sylvester MD, Zhang YB, Berthomieu C, Van Der Lelie D, Matin A. Crystal Structure of ChrR-A Quinone Reductase with the Capacity to Reduce Chromate. PLoS One. 2012;7(4):e36017. Epub 2012 Apr 27. PMID:22558308 doi:10.1371/journal.pone.0036017
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