1IPE

TROPINONE REDUCTASE-II COMPLEXED WITH NADPH

1IPE の概要

• エントリーDOI: 10.2210/pdb1ipe/pdb
• 関連するPDBエントリー: 1IPF
• 分子名称: TROPINONE REDUCTASE-II, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: oxidoreductase, tropane alkaloid biosynthesis, reduction of tropinone to pseudotropine, short-chain dehydrogenase, laue diffraction, riken structural genomics/proteomics initiative, rsgi, structural genomics
• 由来する生物種: Datura stramonium (jimsonweed)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57907.34

構造登録者

Yamashita, A.,Endo, M.,Higashi, T.,Nakatsu, T.,Yamada, Y.,Oda, J.,Kato, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2001-05-09, 公開日: 2003-06-03, 最終更新日: 2023-10-25)

主引用文献

Yamashita, A.,Endo, M.,Higashi, T.,Nakatsu, T.,Yamada, Y.,Oda, J.,Kato, H.
Capturing Enzyme Structure Prior to Reaction Initiation: Tropinone Reductase-II-Substrate Complexes
BIOCHEMISTRY, 42:5566-5573, 2003

PubMed Abstract: 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.

PubMed: 12741812
DOI: 10.1021/bi0272712

実験手法

X-RAY DIFFRACTION (2.5 Å)