2mo1
From Proteopedia
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| ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7== | ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7== | ||
| - | <StructureSection load='2mo1' size='340' side='right'caption='[[2mo1 | + | <StructureSection load='2mo1' size='340' side='right'caption='[[2mo1]]' scene=''> | 
| == Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MO1 FirstGlance]. <br> | 
| - | </td></tr> | + | </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=2mo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mo1 OCA], [https://pdbe.org/2mo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mo1 RCSB], [https://www.ebi.ac.uk/pdbsum/2mo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mo1 ProSAT]</span></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=2mo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mo1 OCA], [https://pdbe.org/2mo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mo1 RCSB], [https://www.ebi.ac.uk/pdbsum/2mo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mo1 ProSAT]</span></td></tr> | + | |
| </table> | </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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2mo1" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
| __TOC__ | __TOC__ | ||
| </StructureSection> | </StructureSection> | ||
| [[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Jeong | + | [[Category: Jeong KW]] | 
| - | [[Category: Jin | + | [[Category: Jin B]] | 
| - | [[Category: Kim | + | [[Category: Kim Y]] | 
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Revision as of 10:23, 31 August 2022
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7
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Categories: Large Structures | Jeong KW | Jin B | Kim Y
