Open AccessSolution NMR structure of the cold‐shock protein from the hyperthermophilic bacterium Thermotoga maritima
Author(s) -
Kremer Werner,
Schuler Benjamin,
Harrieder Stefan,
Geyer Matthias,
Gronwald Wolfram,
Welker Christine,
Jaenicke Rainer,
Kalbitzer Hans R.
Publication year - 2001
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2001.02127.x
Subject(s) - thermotoga maritima , antiparallel (mathematics) , cold shock domain , thermophile , heat shock protein , bacteria , protein structure , chemistry , thermostability , biochemistry , crystallography , rna , biology , escherichia coli , genetics , physics , enzyme , quantum mechanics , magnetic field , gene
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 Tm Csp 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 Tm Csp is based on the peripheral ion cluster around the side chain of R2.