1g6p
From Proteopedia
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| - | [[Image:1g6p.jpg|left|200px]] | + | [[Image:1g6p.jpg|left|200px]] |
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| - | '''SOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA''' | + | {{Structure |
| + | |PDB= 1g6p |SIZE=350|CAPTION= <scene name='initialview01'>1g6p</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G6P is a [ | + | 1G6P is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11322871 11322871] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: ob-fold]] | [[Category: ob-fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:05 2008'' |
Revision as of 09:19, 20 March 2008
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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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