Anders Bergkvist - Transhydrogenase
Transhydrogenase
This project was started in 1997 in cooperation with Prof. Jan Rydström
and coworkers. Transhydrogenase is a membrane-bound enzyme that couples the
reversible reduction of NADP+ by NADH to a proton translocation
across the cytoplasmic membrane. The protein is composed of three domains, the
NAD(H)-binding domain I, the membrane-spanning domain II and the
NADP(H)-binding domain III.
We have cloned and expressed both soluble domains of E. coli
transhydrogenase, ecI (dimer of 2´42.8 kDa)
and ecIII (monomer of 20.4 kDa). We have published an essentially complete
backbone assignment of ecIII and we also have a publication on its global
fold and substrate-binding site. Currently we are working on interaction
studies between ecIII and ecI, and the application of residual dipolar
couplings for the structure determination of ecIII.
Existing publications:
"Sequential assignment and secondary structure analysis of the
NADP(H)-binding domain of Escherichia coli transhydrogenase",
C Johansson, A Bergkvist, O Fjellström, J Rydström and
B G Karlsson, J. Biomol. NMR 14 (1999), 295-296.
"NMR Characterization of the NADP(H)-binding Domain of Eschericia
coli Transhydrogenase; Sequential Assignment and Global Fold",
C Johansson, A Bergkvist, O Fjellström, J Rydström and
B G Karlsson, FEBS Lett. 458 (1999), 180-184.
Publications in prepation:
"Domain Interactions in Transhydrogenase studied by NMR and
Mutagenesis", A Bergkvist, C Johansson, T Johansson,
J Rydström and B G Karlsson. Will be submitted to Biochemistry
during autumn of 1999.
"Residual Dipolar Coupling Measurements in the NADP(H)-binding domain of
Escherichia coli transhydrogenase", A Bergkvist,
T Papavoine, T Johansson, M Billeter and B G Karlsson. Will be submitted
during spring of 2000.
Last modified: November 17, 1999