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| | ==B.subtilis YvgN== | | ==B.subtilis YvgN== |
| - | <StructureSection load='3f7j' size='340' side='right' caption='[[3f7j]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3f7j' size='340' side='right'caption='[[3f7j]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3f7j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3b3e 3b3e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F7J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3f7j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3b3e 3b3e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F7J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b3d|3b3d]], [[3b3f|3b3f]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yvgN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=3f7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f7j OCA], [https://pdbe.org/3f7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f7j RCSB], [https://www.ebi.ac.uk/pdbsum/3f7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f7j ProSAT]</span></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=3f7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f7j OCA], [http://pdbe.org/3f7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f7j RCSB], [http://www.ebi.ac.uk/pdbsum/3f7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f7j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GR_BACSU GR_BACSU]] Reduces glyoxal and methylglyoxal. Is not involved in the vitamin B6 biosynthesis. | + | [https://www.uniprot.org/uniprot/GR_BACSU GR_BACSU] Reduces glyoxal and methylglyoxal. Is not involved in the vitamin B6 biosynthesis. |
| | == 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: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Lei, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Liang, Y H]] | + | [[Category: Lei J]] |
| - | [[Category: Su, X D]] | + | [[Category: Liang YH]] |
| - | [[Category: Zhou, Y F]] | + | [[Category: Su X-D]] |
| - | [[Category: Aldo-keto reductase]]
| + | [[Category: Zhou YF]] |
| - | [[Category: Oxidoreductase]] | + | |
| Structural highlights
Function
GR_BACSU Reduces glyoxal and methylglyoxal. Is not involved in the vitamin B6 biosynthesis.
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
Bacillus subtilis is one of the most studied gram-positive bacteria. In this work, YvgN and YtbE from B. subtilis, assigned as AKR5G1 and AKR5G2 of aldo-keto reductase (AKR) superfamily. AKR catalyzes the NADPH-dependent reduction of aldehyde or aldose substrates to alcohols. YvgN and YtbE were studied by crystallographic and enzymatic analyses. The apo structures of these proteins were determined by molecular replacement, and the structure of holoenzyme YvgN with NADPH was also solved, revealing the conformational changes upon cofactor binding. Our biochemical data suggest both YvgN and YtbE have preferential specificity for derivatives of benzaldehyde, such as nitryl or halogen group substitution at the 2 or 4 positions. These proteins also showed broad catalytic activity on many standard substrates of AKR, such as glyoxal, dihydroxyacetone, and DL-glyceraldehyde, suggesting a possible role in bacterial detoxification.
Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis.,Lei J, Zhou YF, Li LF, Su XD Protein Sci. 2009 Aug;18(8):1792-800. PMID:19585557[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lei J, Zhou YF, Li LF, Su XD. Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis. Protein Sci. 2009 Aug;18(8):1792-800. PMID:19585557 doi:http://dx.doi.org/10.1002/pro.178
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