1G6P

SOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA

Summary for 1G6P

• Entry DOI: 10.2210/pdb1g6p/pdb
• NMR Information: BMRB: 4895
• Descriptor: COLD SHOCK PROTEIN TMCSP (1 entity in total)
• Functional Keywords: greek-key, beta barrel, ob-fold, structural genomics
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 7485.57

Authors

Kremer, W.,Schuler, B.,Harrieder, S.,Geyer, M.,Gronwald, W.,Welker, C.,Jaenicke, R.,Kalbitzer, H.R. (deposition date: 2000-11-07, release date: 2001-11-07, Last modification date: 2024-05-22)

Primary citation

Kremer, W.,Schuler, B.,Harrieder, S.,Geyer, M.,Gronwald, W.,Welker, C.,Jaenicke, R.,Kalbitzer, H.R.
Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Eur.J.Biochem., 268:2527-2539, 2001

PubMed Abstract: 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 beta strands combined in two antiparallel beta sheets making up a beta barrel structure, in which beta 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.

PubMed: 11322871
DOI: 10.1046/j.1432-1327.2001.02127.x

Experimental method

SOLUTION NMR