1ae1
From Proteopedia
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'''TROPINONE REDUCTASE-I COMPLEX WITH NADP''' | '''TROPINONE REDUCTASE-I COMPLEX WITH NADP''' | ||
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[[Category: Yamada, Y.]] | [[Category: Yamada, Y.]] | ||
[[Category: Yamashita, A.]] | [[Category: Yamashita, A.]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Reduction of tropinone to tropine]] |
| - | [[Category: | + | [[Category: Short-chain dehydrogenase]] |
| - | [[Category: | + | [[Category: Tropane alkaloid biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:08:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:08, 2 May 2008
TROPINONE REDUCTASE-I COMPLEX WITH NADP
Overview
A pair of tropinone reductases (TRs) share 64% of the same amino acid residues and belong to the short-chain dehydrogenase/reductase family. In the synthesis of tropane alkaloids in several medicinal plants, the TRs reduce a carbonyl group of an alkaloid intermediate, tropinone, to hydroxy groups with different diastereomeric configurations. To clarify the structural basis for their different reaction stereospecificities, we determined the crystal structures of the two enzymes at 2.4- and 2.3-A resolutions. The overall folding of the two enzymes was almost identical. The conservation was not confined within the core domains that are conserved within the protein family but extended outside the core domain where each family member has its characteristic structure. The binding sites for the cofactor and the positions of the active site residues were well conserved between the two TRs. The substrate binding site was composed mostly of hydrophobic amino acids in both TRs, but the presence of different charged residues conferred different electrostatic environments on the two enzymes. A modeling study indicated that these charged residues play a major role in controlling the binding orientation of tropinone within the substrate binding site, thereby determining the stereospecificity of the reaction product. The results obtained herein raise the possibility that in certain cases different stereospecificities can be acquired in enzymes by changing a few amino acid residues within substrate binding sites.
About this Structure
1AE1 is a Single protein structure of sequence from Datura stramonium. Full crystallographic information is available from OCA.
Reference
Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold., Nakajima K, Yamashita A, Akama H, Nakatsu T, Kato H, Hashimoto T, Oda J, Yamada Y, Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4876-81. PMID:9560196 Page seeded by OCA on Fri May 2 10:08:42 2008
