Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima
Article first published online: 20 DEC 2001
European Journal of Biochemistry
Volume 268, Issue 9, pages 2527–2539, May 2001
How to Cite
Kremer, W., Schuler, B., Harrieder, S., Geyer, M., Gronwald, W., Welker, C., Jaenicke, R. and Kalbitzer, H. R. (2001), Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima. European Journal of Biochemistry, 268: 2527–2539. doi: 10.1046/j.1432-1327.2001.02127.x
- Issue published online: 20 DEC 2001
- Article first published online: 20 DEC 2001
- (Received 14 November 200, revised 12 February 2001, accepted 23 February 2001)
- cold-shock protein;
- NMR spectroscopy;
- structure determination;
- Thermotoga maritima.
Cold-shock proteins (Csps) are a subgroup of the cold-induced proteins preferentially expressed in bacteria and other organisms on reduction of the growth temperature below the physiological temperature. They are related to the cold-shock domain found in eukaryotes and are some of the most conserved proteins known. Their exact function is still not known, but translational regulation, possibly via RNA chaperoning, has been discussed. Here we present the structure of a hyperthermophilic member of the Csp family. The NMR solution structure of TmCsp from Thermotoga maritima, the hyperthermophilic member of this class of proteins, was solved on the basis of 1015 conformational constraints. It contains five β strands combined in two antiparallel β sheets making up a β barrel structure, in which β strands 1–4 are arranged in a Greek-key topology. The side chain of R2, which is exclusively found in thermophilic members of the Csp family, probably participates in a peripheral ion cluster involving residues D20, R2, E47 and K63, suggesting that the thermostability of TmCsp is based on the peripheral ion cluster around the side chain of R2.