NMR characterization of the NADP(H)-binding domain of Escherichia coli transhydrogenase: sequential assignment and global fold.
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.
Johansson
C
C
Department of Biochemistry and Biophysics, Göteborg University, Sweden.
Bergkvist
A
A
Fjellström
O
O
Rydström
J
J
Karlsson
B G
BG
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D002247:Carbon Isotopes; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009249:NADP / Q000737:chemistry* / Q000378:metabolism; D009250:NADP Transhydrogenases / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012247:Rhodospirillum rubrum / Q000201:enzymology; D013379:Substrate Specificity; D013816:Thermodynamics
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D009249:NADP; D009250:NADP Transhydrogenases