4D3D

Structure of Imine Reductase BcSIRED from Bacillus cereus BAG3X2

Summary for 4D3D

• Entry DOI: 10.2210/pdb4d3d/pdb
• Related: 4D3F 4D3S
• Descriptor: IMINE REDUCTASE, MAGNESIUM ION, O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: sired, oxidoreductase
• Biological source: BACILLUS CEREUS
• Total number of polymer chains: 2
• Total formula weight: 68609.54

Authors

Man, H.,Hart, S.,Turkenburg, J.P.,Grogan, G. (deposition date: 2014-10-21, release date: 2015-04-01, Last modification date: 2023-12-20)

Primary citation

Man, H.,Wells, E.,Hussain, S.,Leipold, F.,Hart, S.,Turkenburg, J.P.,Turner, N.J.,Grogan, G.
Structure, Activity and Stereoselectivity of Nadph-Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline.
Chembiochem, 16:1052-, 2015

PubMed Abstract: Oxidoreductases from Streptomyces sp. GF3546 [3546-IRED], Bacillus cereus BAG3X2 (BcIRED) and Nocardiopsis halophila (NhIRED) each reduce prochiral 2-methylpyrroline (2MPN) to (S)-2-methylpyrrolidine with >95 % ee and also a number of other imine substrates with good selectivity. Structures of BcIRED and NhIRED have helped to identify conserved active site residues within this subgroup of imine reductases that have S selectivity towards 2MPN, including a tyrosine residue that has a possible role in catalysis and superimposes with an aspartate in related enzymes that display R selectivity towards the same substrate. Mutation of this tyrosine residue-Tyr169-in 3546-IRED to Phe resulted in a mutant of negligible activity. The data together provide structural evidence for the location and significance of the Tyr residue in this group of imine reductases, and permit a comparison of the active sites of enzymes that reduce 2MPN with either R or S selectivity.

PubMed: 25809902
DOI: 10.1002/CBIC.201402625

Experimental method

X-RAY DIFFRACTION (1.71 Å)