3ZHB: R-imine Reductase From Streptomyces Kanamyceticus In Complex With Nadp

Citation:
Abstract
NADPH-dependent oxidoreductase Q1EQE0 from Streptomyces kanamyceticus catalyzes the asymmetric reduction of the prochiral monocyclic imine 2-methyl-1-pyrroline to the chiral amine (R)-2-methylpyrrolidine with >99 % ee, and is thus of interest as a potential biocatalyst for the production of optically active amines. The structures of Q1EQE0 in native form, and in complex with the nicotinamide cofactor NADPH have been solved and refined to a resolution of 2.7 A. Q1EQE0 functions as a dimer in which the monomer consists of an N-terminal Rossman-fold motif attached to a helical C-terminal domain through a helix of 28 amino acids. The dimer is formed through reciprocal domain sharing in which the C-terminal domains are swapped, with a substrate-binding cleft formed between the N-terminal subunit of monomer A and the C-terminal subunit of monomer B. The structure is related to those of known beta-hydroxyacid dehydrogenases, except that the essential lysine, which serves as an acid/base in the (de)protonation of the nascent alcohol in those enzymes, is replaced by an aspartate residue, Asp187 in Q1EQE0. Mutation of Asp187 to either asparagine or alanine resulted in an inactive enzyme.
PDB ID: 3ZHBDownload
MMDB ID: 111742
PDB Deposition Date: 2012/12/20
Updated in MMDB: 2013/08
Experimental Method:
x-ray diffraction
Resolution: 2.73  Å
Source Organism:
Similar Structures:
Biological Unit for 3ZHB: dimeric; determined by author and by software (PISA)
Molecular Components in 3ZHB
Label Count Molecule
Proteins (2 molecules)
2
R-imine Reductase
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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