|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5az1' size='340' side='right'caption='[[5az1]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5az1' size='340' side='right'caption='[[5az1]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5az1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5az1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5az0|5az0]]</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=5az1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5az1 OCA], [https://pdbe.org/5az1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5az1 RCSB], [https://www.ebi.ac.uk/pdbsum/5az1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5az1 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LOC101740031 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 BOMMO])</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=5az1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5az1 OCA], [http://pdbe.org/5az1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5az1 RCSB], [http://www.ebi.ac.uk/pdbsum/5az1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5az1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 22: |
Line 20: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bommo]] | + | [[Category: Bombyx mori]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Higashiura, A]] | + | [[Category: Higashiura A]] |
| - | [[Category: Nakagawa, A]] | + | [[Category: Nakagawa A]] |
| - | [[Category: Suzuki, M]] | + | [[Category: Suzuki M]] |
| - | [[Category: Yamamoto, K]] | + | [[Category: Yamamoto K]] |
| - | [[Category: Enzyme specificity]]
| + | |
| - | [[Category: Lepidoptera]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
We report a new member of the aldo-keto reductase (AKR) superfamily in the silkworm Bombyx mori. Based on its amino acid sequence, the new enzyme belongs to the AKR2 family and was previously assigned the systematic name AKR2E5. In the present study, recombinant AKR2E5 was expressed, purified to homogeneity, and characterized. The X-ray crystal structures were determined at 2.2 A for the apoenzyme and at 2.3 A resolution for the NADPH-AKR2E5 complex. Our results demonstrate that AKR2E5 is a 40-kDa monomer and includes the TIM- or (beta/alpha)8-barrel typical for other AKRs. We found that AKR2E5 uses NADPH as a cosubstrate to reduce carbonyl compounds such as DL-glyceraldehyde, xylose, 3-hydroxy benzaldehyde, 17alpha-hydroxy progesterone, 11-hexadecenal, and bombykal. No NADH-dependent activity was detected. Site-directed mutagenesis of AKR2E5 indicates that amino acid residues Asp70, Tyr75, Lys104, and His137 contribute to catalytic activity, which is consistent with the data on other AKRs. To the best of our knowledge, AKR2E5 is only the second AKR characterized in silkworm. Our data should contribute to further understanding of the functional activity of insect AKRs.
Structural characterization of an aldo-keto reductase (AKR2E5) from the silkworm Bombyx mori.,Yamamoto K, Higashiura A, Suzuki M, Shiotsuki T, Sugahara R, Fujii T, Nakagawa A Biochem Biophys Res Commun. 2016 May 20;474(1):104-10. doi:, 10.1016/j.bbrc.2016.04.079. Epub 2016 Apr 19. PMID:27103441[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamamoto K, Higashiura A, Suzuki M, Shiotsuki T, Sugahara R, Fujii T, Nakagawa A. Structural characterization of an aldo-keto reductase (AKR2E5) from the silkworm Bombyx mori. Biochem Biophys Res Commun. 2016 May 20;474(1):104-10. doi:, 10.1016/j.bbrc.2016.04.079. Epub 2016 Apr 19. PMID:27103441 doi:http://dx.doi.org/10.1016/j.bbrc.2016.04.079
|
