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| | ==TROPINONE REDUCTASE-II COMPLEXED WITH NADPH== | | ==TROPINONE REDUCTASE-II COMPLEXED WITH NADPH== |
| - | <StructureSection load='1ipe' size='340' side='right' caption='[[1ipe]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='1ipe' size='340' side='right'caption='[[1ipe]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ipe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_thornapple Common thornapple]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IPE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ipe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Datura_stramonium Datura stramonium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IPE 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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ipf|1ipf]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tropinone_reductase_II Tropinone reductase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.236 1.1.1.236] </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=1ipe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ipe OCA], [https://pdbe.org/1ipe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ipe RCSB], [https://www.ebi.ac.uk/pdbsum/1ipe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ipe ProSAT], [https://www.topsan.org/Proteins/RSGI/1ipe TOPSAN]</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=1ipe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ipe OCA], [http://pdbe.org/1ipe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ipe RCSB], [http://www.ebi.ac.uk/pdbsum/1ipe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ipe ProSAT], [http://www.topsan.org/Proteins/RSGI/1ipe TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRN2_DATST TRN2_DATST]] Catalyzes the stereospecific reduction of tropinone to pseudotropine. | + | [https://www.uniprot.org/uniprot/TRN2_DATST TRN2_DATST] Catalyzes the stereospecific reduction of tropinone to pseudotropine. |
| | == 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: Common thornapple]] | + | [[Category: Datura stramonium]] |
| - | [[Category: Tropinone reductase II]] | + | [[Category: Large Structures]] |
| - | [[Category: Endo, M]] | + | [[Category: Endo M]] |
| - | [[Category: Higashi, T]] | + | [[Category: Higashi T]] |
| - | [[Category: Kato, H]] | + | [[Category: Kato H]] |
| - | [[Category: Nakatsu, T]] | + | [[Category: Nakatsu T]] |
| - | [[Category: Oda, J]] | + | [[Category: Oda J]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Yamada Y]] |
| - | [[Category: Yamada, Y]] | + | [[Category: Yamashita A]] |
| - | [[Category: Yamashita, A]] | + | |
| - | [[Category: Laue diffraction]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Reduction of tropinone to pseudotropine]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Short-chain dehydrogenase]]
| + | |
| - | [[Category: Tropane alkaloid biosynthesis]]
| + | |
| Structural highlights
Function
TRN2_DATST Catalyzes the stereospecific reduction of tropinone to pseudotropine.
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
To understand the catalytic mechanism of an enzyme, it is crucial to determine the crystallographic structures corresponding to the individual reaction steps. Here, we report two crystal structures of enzyme-substrate complexes prior to reaction initiation: tropinone reductase-II (TR-II)-NADPH and TR-II-NADPH-tropinone complexes, determined from the identical crystals. A combination of two kinetic crystallographic techniques, a continuous flow of the substrates and Laue diffraction measurements, enabled us to capture the transit structures prior to the reaction proceeding. A structure comparison of the enzyme-substrate complex elucidated in this study with the enzyme-product complex in our previous study indicates that one of the substrates, tropinone, is rotated relative to the product so as to make the spatial organization in the active site favorable for the reaction to proceed. Side chains of the residues in the active site also alter their conformations to keep the complementarity of the space for the substrate or the product and to assist the rotational movement.
Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes.,Yamashita A, Endo M, Higashi T, Nakatsu T, Yamada Y, Oda J, Kato H Biochemistry. 2003 May 20;42(19):5566-73. PMID:12741812[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamashita A, Endo M, Higashi T, Nakatsu T, Yamada Y, Oda J, Kato H. Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes. Biochemistry. 2003 May 20;42(19):5566-73. PMID:12741812 doi:10.1021/bi0272712
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