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| | <StructureSection load='2q7v' size='340' side='right'caption='[[2q7v]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2q7v' size='340' side='right'caption='[[2q7v]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2q7v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q7V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2q7v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q7V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TrxB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 "Micrococcus radiodurans" Raj et al. 1960])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2q7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q7v OCA], [https://pdbe.org/2q7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q7v RCSB], [https://www.ebi.ac.uk/pdbsum/2q7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q7v 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=2q7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q7v OCA], [https://pdbe.org/2q7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q7v RCSB], [https://www.ebi.ac.uk/pdbsum/2q7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q7v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RSY7_DEIRA Q9RSY7_DEIRA] |
| | == 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: Micrococcus radiodurans raj et al. 1960]] | + | [[Category: Deinococcus radiodurans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thioredoxin-disulfide reductase]]
| + | [[Category: Bonderoff SA]] |
| - | [[Category: Bonderoff, S A]] | + | [[Category: Goertzen MM]] |
| - | [[Category: Goertzen, M M]] | + | [[Category: Obiero J]] |
| - | [[Category: Obiero, J]] | + | [[Category: Sanders DAR]] |
| - | [[Category: Sanders, D A.R]] | + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q9RSY7_DEIRA
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
This paper describes the cloning, purification, and characterization of thioredoxin (Trx) and thioredoxin reductase (TrxR) and the structure determination of TrxR from the ionizing radiation-tolerant bacterium Deinococcus radiodurans strain R1. The genes from D. radiodurans encoding Trx and TrxR were amplified by PCR, inserted into a pET expression vector, and overexpressed in Escherichia coli. The overexpressed proteins were purified by metal affinity chromatography, and their activity was demonstrated using well-established assays of insulin precipitation (for Trx), 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) reduction, and insulin reduction (for TrxR). In addition, the crystal structure of oxidized TrxR was determined at 1.9-A resolution. The overall structure was found to be very similar to that of E. coli TrxR and homodimeric with both NADPH- and flavin adenine dinucleotide (FAD)-binding domains containing variants of the canonical nucleotide binding fold, the Rossmann fold. The K(m) (5.7 muM) of D. radiodurans TrxR for D. radiodurans Trx was determined and is about twofold higher than that of the E. coli thioredoxin system. However, D. radiodurans TrxR has a much lower affinity for E. coli Trx (K(m), 44.4 muM). Subtle differences in the surface charge and shape of the Trx binding site on TrxR may account for the differences in recognition. Because it has been suggested that TrxR from D. radiodurans may have dual cofactor specificity (can utilize both NADH and NADPH), D. radiodurans TrxR was tested for its ability to utilize NADH as well. Our results show that D. radiodurans TrxR can utilize only NADPH for activity.
Thioredoxin system from Deinococcus radiodurans.,Obiero J, Pittet V, Bonderoff SA, Sanders DA J Bacteriol. 2010 Jan;192(2):494-501. Epub 2009 Nov 20. PMID:19933368[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Obiero J, Pittet V, Bonderoff SA, Sanders DA. Thioredoxin system from Deinococcus radiodurans. J Bacteriol. 2010 Jan;192(2):494-501. Epub 2009 Nov 20. PMID:19933368 doi:10.1128/JB.01046-09
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