3svl

From Proteopedia

(Difference between revisions)

Revision as of 08:12, 29 June 2022

Structural basis of the improvement of ChrR - a multi-purpose enzyme

Structural highlights

3svl is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	yieF, b3713, JW3691 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3svl"

@@ Line 1: / Line 1: @@
 ==Structural basis of the improvement of ChrR - a multi-purpose enzyme==
-<StructureSection load='3svl' size='340' side='right' caption='[[3svl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3svl' size='340' side='right'caption='[[3svl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3svl]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yieF, b3713, JW3691 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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='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=3svl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3svl OCA], [http://pdbe.org/3svl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3svl RCSB], [http://www.ebi.ac.uk/pdbsum/3svl PDBsum], [http://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>
 == Function ==
-[[http://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 ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Ecoli]]
+[[Category: Large Structures]]
 [[Category: Berthomieu, C]]
 [[Category: Bremond, N]]

3svl

From Proteopedia

Revision as of 08:12, 29 June 2022

Structural basis of the improvement of ChrR - a multi-purpose enzyme

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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