2mo0: Difference between revisions
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<StructureSection load='2mo0' size='340' side='right'caption='[[2mo0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2mo0' size='340' side='right'caption='[[2mo0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mo0]] is a 1 chain structure | <table><tr><td colspan='2'>[[2mo0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MO0 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mo1|2mo1]]</div></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mo1|2mo1]]</div></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=2mo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mo0 OCA], [https://pdbe.org/2mo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mo0 RCSB], [https://www.ebi.ac.uk/pdbsum/2mo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mo0 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=2mo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mo0 OCA], [https://pdbe.org/2mo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mo0 RCSB], [https://www.ebi.ac.uk/pdbsum/2mo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mo0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jeong, K W]] | [[Category: Jeong, K W]] | ||
[[Category: Jin, B]] | [[Category: Jin, B]] | ||
Revision as of 07:55, 25 August 2022
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCspBackbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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