5xv9
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of Cold Shock Protein from Colwellia psychrerythraea== | |
| + | <StructureSection load='5xv9' size='340' side='right' caption='[[5xv9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xv9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XV9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xv9 OCA], [http://pdbe.org/5xv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5xv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xv9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The thermophilic bacterium Thermus aquaticus is a well-known source of Taq polymerase. Here, we studied the structure and dynamics of the T. aquaticus cold-shock protein (Ta-Csp) to better understand its thermostability using NMR spectroscopy. We found that Ta-Csp has a five-stranded beta-barrel structure with five salt bridges which are important for more rigid structure and a higher melting temperature (76 degrees C) of Ta-Csp compared to mesophilic and psychrophilic Csps. Microsecond to millisecond time scale exchange processes occur only at the beta1-beta2 surface region of the nucleic acid binding site with an average conformational exchange rate constant of 674s-1. The results imply that thermophilic Ta-Csp has a more rigid structure and may not need high structural flexibility to accommodate nucleic acids upon cold shock compared to its mesophile and psychrophile counterparts. | ||
| - | + | Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus.,Jin B, Jeong KW, Kim Y Biochem Biophys Res Commun. 2014 Aug 4. pii: S0006-291X(14)01377-1. doi:, 10.1016/j.bbrc.2014.07.127. PMID:25101648<ref>PMID:25101648</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5xv9" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Kim, Y]] | [[Category: Kim, Y]] | ||
| + | [[Category: Lee, Y]] | ||
| + | [[Category: Cold-shock protein]] | ||
| + | [[Category: Nmr spectroscopy]] | ||
| + | [[Category: Psychrophile]] | ||
| + | [[Category: Rna binding protein]] | ||
| + | [[Category: Solution structure]] | ||
Revision as of 07:07, 4 July 2018
Solution Structure of Cold Shock Protein from Colwellia psychrerythraea
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