4O0L

Crystal structure of NADPH-Dependent 3-Quinuclidinone Reductase from Rhodotorula Rubra

Summary for 4O0L

• Entry DOI: 10.2210/pdb4o0l/pdb
• Descriptor: NADPH-dependent 3-quinuclidinone reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: rossmann fold, oxidoreductase
• Biological source: Rhodotorula mucilaginosa
• Total number of polymer chains: 4
• Total formula weight: 120501.67

Authors

Takeshita, D.,Tanokura, M. (deposition date: 2013-12-13, release date: 2014-08-13, Last modification date: 2023-11-08)

Primary citation

Takeshita, D.,Kataoka, M.,Miyakawa, T.,Miyazono, K.,Kumashiro, S.,Nagai, T.,Urano, N.,Uzura, A.,Nagata, K.,Shimizu, S.,Tanokura, M.
Structural basis of stereospecific reduction by quinuclidinone reductase
AMB Express, 4:6-6, 2014

PubMed Abstract: Chiral molecule (R)-3-quinuclidinol, a valuable compound for the production of various pharmaceuticals, is efficiently synthesized from 3-quinuclidinone by using NADPH-dependent 3-quinuclidinone reductase (RrQR) from Rhodotorula rubra. Here, we report the crystal structure of RrQR and the structure-based mutational analysis. The enzyme forms a tetramer, in which the core of each protomer exhibits the α/β Rossmann fold and contains one molecule of NADPH, whereas the characteristic substructures of a small lobe and a variable loop are localized around the substrate-binding site. Modeling and mutation analyses of the catalytic site indicated that the hydrophobicity of two residues, I167 and F212, determines the substrate-binding orientation as well as the substrate-binding affinity. Our results revealed that the characteristic substrate-binding pocket composed of hydrophobic amino acid residues ensures substrate docking for the stereospecific reaction of RrQR in spite of its loose interaction with the substrate.

PubMed: 24507746
DOI: 10.1186/2191-0855-4-6

Experimental method

X-RAY DIFFRACTION (2.2 Å)