2mo1
From Proteopedia
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| - | ''' | + | ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7== |
| + | <StructureSection load='2mo1' size='340' side='right' caption='[[2mo1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mo1]] is a 1 chain structure. Full experimental 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MO1 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mo0|2mo0]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mo1 RCSB], [http://www.ebi.ac.uk/pdbsum/2mo1 PDBsum]</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> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Jeong, K W.]] | ||
| + | [[Category: Jin, B.]] | ||
| + | [[Category: Kim, Y.]] | ||
| + | [[Category: Cold shock protein]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Protein stability]] | ||
| + | [[Category: Thermus aquaticus]] | ||
Revision as of 16:23, 20 August 2014
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7
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