1ipe

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|PDB= 1ipe |SIZE=350|CAPTION= <scene name='initialview01'>1ipe</scene>, resolution 2.50&Aring;
|PDB= 1ipe |SIZE=350|CAPTION= <scene name='initialview01'>1ipe</scene>, resolution 2.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene>
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|LIGAND= <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <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>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1ipf|1IPF]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1ipe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ipe RCSB]</span>
}}
}}
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[[Category: Yamada, Y.]]
[[Category: Yamada, Y.]]
[[Category: Yamashita, A.]]
[[Category: Yamashita, A.]]
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[[Category: NDP]]
 
[[Category: laue diffraction]]
[[Category: laue diffraction]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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[[Category: tropane alkaloid biosynthesis]]
[[Category: tropane alkaloid biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:53:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:53 2008''

Revision as of 18:22, 30 March 2008

Image:1ipe.jpg


PDB ID 1ipe

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands:
Activity: Tropinone reductase II, with EC number 1.1.1.236
Related: 1IPF


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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