1g6p

<StructureSection load='1g6p' size='340' side='right'caption='[[1g6p]], [[NMR_Ensembles_of_Models | 7 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1g6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G6P FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6p OCA], [https://pdbe.org/1g6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g6p RCSB], [https://www.ebi.ac.uk/pdbsum/1g6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g6p ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11322871</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1g6p" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: Geyer, M]]

[[Category: Gronwald, W]]

[[Category: Harrieder, S]]

[[Category: Jaenicke, R]]

[[Category: Kalbitzer, H R]]

[[Category: Kremer, W]]

[[Category: Schuler, B]]

[[Category: Welker, C]]

[[Category: Structural genomic]]