2mo1

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<StructureSection load='2mo1' size='340' side='right'caption='[[2mo1]]' scene=''>
<StructureSection load='2mo1' size='340' side='right'caption='[[2mo1]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[2mo1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus_Y51MC23 Thermus aquaticus Y51MC23]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2MO1 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=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>
</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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mo1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thermus aquaticus Y51MC23]]
[[Category: Jeong KW]]
[[Category: Jeong KW]]
[[Category: Jin B]]
[[Category: Jin B]]
[[Category: Kim Y]]
[[Category: Kim Y]]

Revision as of 09:40, 14 June 2023

Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7

PDB ID 2mo1

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