2ae2: Difference between revisions
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<StructureSection load='2ae2' size='340' side='right'caption='[[2ae2]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2ae2' size='340' side='right'caption='[[2ae2]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ae2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2ae2]] 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=2AE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AE2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PTO:PSEUDOTROPINE'>PTO</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=2ae2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae2 OCA], [https://pdbe.org/2ae2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ae2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ae2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ae2 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=2ae2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae2 OCA], [https://pdbe.org/2ae2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ae2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ae2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ae2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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: | [[Category: Datura stramonium]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hashimoto T]] | |||
[[Category: Hashimoto | [[Category: Kato H]] | ||
[[Category: Kato | [[Category: Nakajima K]] | ||
[[Category: Nakajima | [[Category: Nakatsu T]] | ||
[[Category: Nakatsu | [[Category: Oda J]] | ||
[[Category: Oda | [[Category: Tomizaki T]] | ||
[[Category: Tomizaki | [[Category: Wakatsuki S]] | ||
[[Category: Wakatsuki | [[Category: Yamada Y]] | ||
[[Category: Yamada | [[Category: Yamashita A]] | ||
[[Category: Yamashita | |||
Latest revision as of 10:22, 23 August 2023
TROPINONE REDUCTASE-II COMPLEXED WITH NADP+ AND PSEUDOTROPINETROPINONE REDUCTASE-II COMPLEXED WITH NADP+ AND PSEUDOTROPINE
Structural highlights
FunctionTRN2_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 PubMedTropinone reductase-II (TR-II) catalyzes the NADPH-dependent reduction of the carbonyl group of tropinone to a beta-hydroxyl group. The crystal structure of TR-II complexed with NADP+ and pseudotropine (psi-tropine) has been determined at 1.9 A resolution. A seven-residue peptide near the active site, disordered in the unliganded structure, is fixed in the ternary complex by participation of the cofactor and substrate binding. The psi-tropine molecule is bound in an orientation which satisfies the product configuration and the stereochemical arrangement toward the cofactor. The substrate binding site displays a complementarity to the bound substrate (psi-tropine) in its correct orientation. In addition, electrostatic interactions between the substrate and Glu156 seem to specify the binding position and orientation of the substrate. A comparison between the active sites in TR-II and TR-I shows that they provide different van der Waals surfaces and electrostatic features. These differences likely contribute to the correct binding mode of the substrates, which are in opposite orientations in TR-II and TR-I, and to different reaction stereospecificities. The active site structure in the TR-II ternary complex also suggests that the arrangement of the substrate, cofactor, and catalytic residues is stereoelectronically favorable for the reaction. Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis.,Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J Biochemistry. 1999 Jun 15;38(24):7630-7. PMID:10387002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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