Abstract
The soluble NADP(H)-binding domain of Escherichia coli transhydrogenase (186 amino acids, 20.4 kDa, rotational correlation time 14 ns) was characterized using NMR techniques. The global fold is similar to that of a classical dinucleotide-binding fold with six parallel β-strands in a central sheet surrounded by helices and irregular structures, but is lacking both αD and αE. The substrate is bound in an extended conformation at the C-terminal end of the parallel β-sheet and our data support the notion of a redox dependent structural rearrangement.
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