TROPINONE REDUCTASE-II COMPLEXED WITH NADPH

RIKEN Structural Genomics/Proteomics Initiative (RSGI)

NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Capturing Enzyme Structure Prior to Reaction Initiation: Tropinone Reductase-II-Substrate Complexes

Structure of Tropinone Reductase-II Complexed with NADP+ and Pseudotropine at 1.9 A Resolution: Implication for Stereospecific Substrate Binding and Catalysis

Crystal Structures of Two Tropinone Reductases: Different Reaction Stereospecificities in the Same Protein Fold

AGRWNLEGCTALVTGGSRGIGYGIVEELASLGASVYTCSRNQKELNDCLTQWRSKGFKVEASVCDLSSRSERQELMNTVA
NHFHGKLNILVNNAGIVIYKEAKDYTVEDYSLIMSINFEAAYHLSVLAHPFLKASERGNVVFISSVSGALAVPYEAVYGA
TKGAMDQLTRCLAFEWAKDNIRVNGVGPGVIATSLVEMTIQDPEQKENLNKLIDRCALRRMGEPKELAAMVAFLCFPAAS
YVTGQIIYVDGGLMANCGF

lithium sulfate, dithiothreitol, HEPES, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 289.0K

RIKEN Structural Genomics/Proteomics Initiative

1IPF contains the same protein complexed with NADPH and TROPINONE

This solvent would make a 3.5 A hydrogen bond with HOH 26, which makes a hydrogen bond with protein molecule with 3.4 A distance.

OXIDOREDUCTASE, TROPANE ALKALOID BIOSYNTHESIS, REDUCTION OF TROPINONE TO PSEUDOTROPINE, SHORT-CHAIN DEHYDROGENASE, LAUE DIFFRACTION, RIKEN Structural Genomics/Proteomics Initiative, RSGI, Structural Genomics