4o0l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of NADPH-Dependent 3-Quinuclidinone Reductase from Rhodotorula Rubra== | |
| + | <StructureSection load='4o0l' size='340' side='right'caption='[[4o0l]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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'>[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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B9ZZZ6_RHOMI B9ZZZ6_RHOMI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24507746</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4o0l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhodotorula mucilaginosa]] | ||
| + | [[Category: Takeshita D]] | ||
| + | [[Category: Tanokura M]] | ||
Current revision
Crystal structure of NADPH-Dependent 3-Quinuclidinone Reductase from Rhodotorula Rubra
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