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| | <StructureSection load='2rg1' size='340' side='right'caption='[[2rg1]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='2rg1' size='340' side='right'caption='[[2rg1]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rg1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RG1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rg1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RG1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r96|2r96]], [[2r97|2r97]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wrbA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] </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=2rg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rg1 OCA], [https://pdbe.org/2rg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2rg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rg1 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=2rg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rg1 OCA], [https://pdbe.org/2rg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2rg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rg1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NQOR_ECOLI NQOR_ECOLI]] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.<ref>PMID:16672604</ref> <ref>PMID:9694845</ref>
| + | [https://www.uniprot.org/uniprot/NQOR_ECOLI NQOR_ECOLI] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.<ref>PMID:16672604</ref> <ref>PMID:9694845</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brynda, J]] | + | [[Category: Brynda J]] |
| - | [[Category: Carey, J]] | + | [[Category: Carey J]] |
| - | [[Category: Grandori, R]] | + | [[Category: Grandori R]] |
| - | [[Category: Lapkouski, M]] | + | [[Category: Kuta Smatanova I]] |
| - | [[Category: Mesters, J R]] | + | [[Category: Lapkouski M]] |
| - | [[Category: Smatanova, I Kuta]] | + | [[Category: Mesters JR]] |
| - | [[Category: Wolfova, J]] | + | [[Category: Wolfova J]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Flavodoxin-like fold]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Fmn-binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Quinone oxidoreductase]]
| + | |
| Structural highlights
Function
NQOR_ECOLI It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Two previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 A resolution, and new crystals of WrbA apoprotein diffracting to 1.85 A, are refined and analysed comparatively through the lens of flavodoxin structures. The results indicate that differences between apo- and holoWrbA crystal structures are manifested on many levels of protein organization as well as in the FMN-binding sites. Evaluation of the influence of crystal contacts by comparison of lattice packing reveals the protein's global response to FMN binding. Structural changes upon cofactor binding are compared with the monomeric flavodoxins. Topologically non-equivalent residues undergo remarkably similar local structural changes upon FMN binding to WrbA or to flavodoxin, despite differences in multimeric organization and residue types at the binding sites. Analysis of the three crystal structures described here, together with flavodoxin structures, rationalizes functional similarities and differences of the WrbAs relative to flavodoxins, leading to a new understanding of the defining features of WrbAs. The results suggest that WrbAs are not a remote and unusual branch of the flavodoxin family as previously thought but rather a central member with unifying structural features.
Structural organization of WrbA in apo- and holoprotein crystals.,Wolfova J, Smatanova IK, Brynda J, Mesters JR, Lapkouski M, Kuty M, Natalello A, Chatterjee N, Chern SY, Ebbel E, Ricci A, Grandori R, Ettrich R, Carey J Biochim Biophys Acta. 2009 Sep;1794(9):1288-98. Epub 2009 Aug 7. PMID:19665595[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Patridge EV, Ferry JG. WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase. J Bacteriol. 2006 May;188(10):3498-506. PMID:16672604 doi:http://dx.doi.org/10.1128/JB.188.10.3498-3506.2006
- ↑ Grandori R, Khalifah P, Boice JA, Fairman R, Giovanielli K, Carey J. Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins. J Biol Chem. 1998 Aug 14;273(33):20960-6. PMID:9694845
- ↑ Wolfova J, Smatanova IK, Brynda J, Mesters JR, Lapkouski M, Kuty M, Natalello A, Chatterjee N, Chern SY, Ebbel E, Ricci A, Grandori R, Ettrich R, Carey J. Structural organization of WrbA in apo- and holoprotein crystals. Biochim Biophys Acta. 2009 Sep;1794(9):1288-98. Epub 2009 Aug 7. PMID:19665595 doi:10.1016/j.bbapap.2009.08.001
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