1g6p

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(New page: 200px<br /><applet load="1g6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g6p" /> '''SOLUTION NMR STRUCTURE OF THE COLD SHOCK PRO...)
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'''SOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA'''<br />
'''SOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1G6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G6P OCA].
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1G6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6P OCA].
==Reference==
==Reference==
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[[Category: Harrieder, S.]]
[[Category: Harrieder, S.]]
[[Category: Jaenicke, R.]]
[[Category: Jaenicke, R.]]
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[[Category: Kalbitzer, H.R.]]
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[[Category: Kalbitzer, H R.]]
[[Category: Kremer, W.]]
[[Category: Kremer, W.]]
[[Category: Schuler, B.]]
[[Category: Schuler, B.]]
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[[Category: ob-fold]]
[[Category: ob-fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:45:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:45 2008''

Revision as of 10:46, 21 February 2008


1g6p

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

Overview

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.

About this Structure

1G6P is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima., Kremer W, Schuler B, Harrieder S, Geyer M, Gronwald W, Welker C, Jaenicke R, Kalbitzer HR, Eur J Biochem. 2001 May;268(9):2527-39. PMID:11322871

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