2ae2
From Proteopedia
(New page: 200px<br /><applet load="2ae2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ae2, resolution 1.90Å" /> '''TROPINONE REDUCTASE-...) |
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| - | [[Image:2ae2.jpg|left|200px]]<br /><applet load="2ae2" size=" | + | [[Image:2ae2.jpg|left|200px]]<br /><applet load="2ae2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ae2, resolution 1.90Å" /> | caption="2ae2, resolution 1.90Å" /> | ||
'''TROPINONE REDUCTASE-II COMPLEXED WITH NADP+ AND PSEUDOTROPINE'''<br /> | '''TROPINONE REDUCTASE-II COMPLEXED WITH NADP+ AND PSEUDOTROPINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tropinone reductase-II (TR-II) catalyzes the NADPH-dependent reduction of | + | Tropinone 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2AE2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Datura_stramonium Datura stramonium] with NAP and PTO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2AE2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Datura_stramonium Datura stramonium] with <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=PTO:'>PTO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AE2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tropane alkaloid biosynthesis]] | [[Category: tropane alkaloid biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:26:25 2008'' |
Revision as of 14:26, 21 February 2008
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TROPINONE REDUCTASE-II COMPLEXED WITH NADP+ AND PSEUDOTROPINE
Overview
Tropinone 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.
About this Structure
2AE2 is a Single protein structure of sequence from Datura stramonium with and as ligands. Active as Tropinone reductase II, with EC number 1.1.1.236 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:26:25 2008
Categories: Datura stramonium | Single protein | Tropinone reductase II | Hashimoto, T. | Kato, H. | Nakajima, K. | Nakatsu, T. | Oda, J. | Tomizaki, T. | Wakatsuki, S. | Yamada, Y. | Yamashita, A. | NAP | PTO | Oxidoreductase | Reduction of tropinone to pseudotropine | Short-chain dehydrogenase | Tropane alkaloid biosynthesis
