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3d3f

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Revision as of 08:41, 25 October 2017

Crystal Structure of Yvgn and cofactor NADPH from Bacillus subtilis

Structural highlights

3d3f is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	yvgN ("Bacillus globigii" Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3d3f"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Yvgn and cofactor NADPH from Bacillus subtilis==
 <StructureSection load='3d3f' size='340' side='right' caption='[[3d3f]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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 "Bacillus globigii" Migula 1900])</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=3d3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d3f OCA], [http://pdbe.org/3d3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d3f RCSB], [http://www.ebi.ac.uk/pdbsum/3d3f PDBsum]</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=3d3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d3f OCA], [http://pdbe.org/3d3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d3f RCSB], [http://www.ebi.ac.uk/pdbsum/3d3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d3f ProSAT]</span></td></tr>
 </table>
 == Function ==

3d3f

From Proteopedia

Revision as of 08:41, 25 October 2017

Crystal Structure of Yvgn and cofactor NADPH from Bacillus subtilis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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