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3ra5

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[[Image:3ra5.jpg|left|200px]]
 
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==Crystal structure of T. celer L30e E6A/R92A variant==
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The line below this paragraph, containing "STRUCTURE_3ra5", creates the "Structure Box" on the page.
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<StructureSection load='3ra5' size='340' side='right'caption='[[3ra5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3ra5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RA5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3ra5| PDB=3ra5 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ra5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ra5 OCA], [https://pdbe.org/3ra5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ra5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ra5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ra5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Most thermophilic proteins tend to have more salt bridges, and achieve higher thermostability by up-shifting and broadening their protein stability curves. While the stabilizing effect of salt-bridge has been extensively studied, experimental data on how salt-bridge influences protein stability curves are scarce. Here, we used double mutant cycles to determine the temperature-dependency of the pair-wise interaction energy and the contribution of salt-bridges to DeltaC(p) in a thermophilic ribosomal protein L30e. Our results showed that the pair-wise interaction energies for the salt-bridges E6/R92 and E62/K46 were stabilizing and insensitive to temperature changes from 298 to 348 K. On the other hand, the pair-wise interaction energies between the control long-range ion-pair of E90/R92 were negligible. The DeltaC(p) of all single and double mutants were determined by Gibbs-Helmholtz and Kirchhoff analyses. We showed that the two stabilizing salt-bridges contributed to a reduction of DeltaC(p) by 0.8-1.0 kJ mol(1) K(1). Taken together, our results suggest that the extra salt-bridges found in thermophilic proteins enhance the thermostability of proteins by reducing DeltaC(p), leading to the up-shifting and broadening of the protein stability curves.
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===Crystal structure of T. celer L30e E6A/R92A variant===
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Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding.,Chan CH, Yu TH, Wong KB PLoS One. 2011;6(6):e21624. Epub 2011 Jun 24. PMID:21720566<ref>PMID:21720566</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 3ra5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 21720566 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21720566}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3ra5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RA5 OCA].
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==Reference==
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<ref group="xtra">PMID:021720566</ref><references group="xtra"/>
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[[Category: Thermococcus celer]]
[[Category: Thermococcus celer]]
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[[Category: Chan, C H.]]
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[[Category: Chan CH]]
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[[Category: Wong, K B.]]
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[[Category: Wong KB]]
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[[Category: Globular protein]]
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[[Category: L30e]]
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[[Category: Ribosomal protein]]
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[[Category: Thermophilic]]
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Current revision

Crystal structure of T. celer L30e E6A/R92A variant

PDB ID 3ra5

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