1ipe
From Proteopedia
(New page: 200px<br /><applet load="1ipe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ipe, resolution 2.50Å" /> '''TROPINONE REDUCTASE-...) |
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| - | [[Image:1ipe.jpg|left|200px]]<br /><applet load="1ipe" size=" | + | [[Image:1ipe.jpg|left|200px]]<br /><applet load="1ipe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ipe, resolution 2.50Å" /> | caption="1ipe, resolution 2.50Å" /> | ||
'''TROPINONE REDUCTASE-II COMPLEXED WITH NADPH'''<br /> | '''TROPINONE REDUCTASE-II COMPLEXED WITH NADPH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To understand the catalytic mechanism of an enzyme, it is crucial to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1IPE 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 NDP as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1IPE 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=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1IPE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nakatsu, T.]] | [[Category: Nakatsu, T.]] | ||
[[Category: Oda, J.]] | [[Category: Oda, J.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yamada, Y.]] | [[Category: Yamada, Y.]] | ||
[[Category: Yamashita, A.]] | [[Category: Yamashita, A.]] | ||
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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 13:14:13 2008'' |
Revision as of 11:14, 21 February 2008
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TROPINONE REDUCTASE-II COMPLEXED WITH NADPH
Overview
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.
About this Structure
1IPE is a Single protein structure of sequence from Datura stramonium with as ligand. Active as Tropinone reductase II, with EC number 1.1.1.236 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:14:13 2008
Categories: Datura stramonium | Single protein | Tropinone reductase II | Endo, M. | Higashi, T. | Kato, H. | Nakatsu, T. | Oda, J. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yamada, Y. | Yamashita, A. | NDP | Laue diffraction | Oxidoreductase | Reduction of tropinone to pseudotropine | Riken structural genomics/proteomics initiative | Rsgi | Short-chain dehydrogenase | Structural genomics | Tropane alkaloid biosynthesis
