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NMR characterization of the NADP(H)-binding domain of Escherichia coli transhydrogenase: sequential assignment and
C Johansson1, A Bergkvist, O Fjellström
1Department of Biochemistry and Biophysics, Göteborg University, Sweden.
FEBS Letters
|September 11, 1999
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 beta-strands in a central sheet surrounded by helices and irregular structures, but is lacking both alphaD and alphaE. The substrate is bound in an extended conformation at the C-terminal end of the parallel beta-sheet and our data support the notion of a redox dependent structural rearrangement.