PMID:10481061

Citation	Johansson, C, Bergkvist, A, Fjellström, O, Rydström, J and Karlsson, BG (1999) NMR characterization of the NADP(H)-binding domain of Escherichia coli transhydrogenase: sequential assignment and global fold. FEBS Lett. 458:180-4
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.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carbon Isotopes; Escherichia coli/enzymology; Escherichia coli/growth & development; Models, Molecular; Molecular Sequence Data; NADP/chemistry; NADP/metabolism; NADP Transhydrogenases/biosynthesis; NADP Transhydrogenases/chemistry; NADP Transhydrogenases/metabolism; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular/methods; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Rhodospirillum rubrum/enzymology; Substrate Specificity; Thermodynamics
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