    1.1.1.283 | more |
Gre2 uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde. The cofactor-binding domain of CaGre2 adopts a typical Rossmann-fold motif, which is a beta-sheet composed of seven parallel beta-strands (beta1-7 with strand topology 3-2-1-4-5-6-7) that form the hydrophobic core of the domain surrounded by nine alpha-helices (alpha1-5, alpha7-8, alpha10, and alpha13) on both sides of the beta-sheet. Additionally, the conserved dinucleotide-binding motif (G11A12T13G14F15I16A17), which is responsible for the binding of NADPH, is exhibited as a loop followed by beta1 and a partial helix of alpha1. The C-terminal substrate-binding domain is formed by five helices (alpha6, alpha9, alpha11-12, and alpha14) and three twisted beta-strands (beta1', beta2', beta3'), with lengths ranging from 5 to 16 and from 3 to 6 residues, respectively |
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