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| | <StructureSection load='4o0l' size='340' side='right'caption='[[4o0l]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4o0l' size='340' side='right'caption='[[4o0l]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o0l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_316 Cbs 316]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o0l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodotorula_mucilaginosa Rhodotorula mucilaginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0L FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rqr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5537 CBS 316])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=4o0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0l OCA], [http://pdbe.org/4o0l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o0l RCSB], [http://www.ebi.ac.uk/pdbsum/4o0l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0l 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=4o0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0l OCA], [https://pdbe.org/4o0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0l RCSB], [https://www.ebi.ac.uk/pdbsum/4o0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B9ZZZ6_RHOMI B9ZZZ6_RHOMI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 316]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Takeshita, D]] | + | [[Category: Rhodotorula mucilaginosa]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Takeshita D]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Tanokura M]] |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
B9ZZZ6_RHOMI
Publication Abstract from PubMed
Chiral molecule (R)-3-quinuclidinol, a valuable compound for the production of various pharmaceuticals, is efficiently synthesized from 3-quinuclidinone by using NADPH-dependent 3-quinuclidinone reductase (RrQR) from Rhodotorula rubra. Here, we report the crystal structure of RrQR and the structure-based mutational analysis. The enzyme forms a tetramer, in which the core of each protomer exhibits the alpha/beta Rossmann fold and contains one molecule of NADPH, whereas the characteristic substructures of a small lobe and a variable loop are localized around the substrate-binding site. Modeling and mutation analyses of the catalytic site indicated that the hydrophobicity of two residues, I167 and F212, determines the substrate-binding orientation as well as the substrate-binding affinity. Our results revealed that the characteristic substrate-binding pocket composed of hydrophobic amino acid residues ensures substrate docking for the stereospecific reaction of RrQR in spite of its loose interaction with the substrate.
Structural basis of stereospecific reduction by quinuclidinone reductase.,Takeshita D, Kataoka M, Miyakawa T, Miyazono K, Kumashiro S, Nagai T, Urano N, Uzura A, Nagata K, Shimizu S, Tanokura M AMB Express. 2014 Feb 7;4(1):6. doi: 10.1186/2191-0855-4-6. PMID:24507746[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takeshita D, Kataoka M, Miyakawa T, Miyazono K, Kumashiro S, Nagai T, Urano N, Uzura A, Nagata K, Shimizu S, Tanokura M. Structural basis of stereospecific reduction by quinuclidinone reductase. AMB Express. 2014 Feb 7;4(1):6. doi: 10.1186/2191-0855-4-6. PMID:24507746 doi:http://dx.doi.org/10.1186/2191-0855-4-6
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