3lfo: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lfo]] is a 1 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=3LFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LFO FirstGlance]. <br> | <table><tr><td colspan='2'>[[3lfo]] is a 1 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=3LFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LFO FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h7m|1h7m]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h7m|1h7m]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpl30e, rpl30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2264 Thermococcus celer])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpl30e, rpl30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2264 Thermococcus celer])</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=3lfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lfo RCSB], [http://www.ebi.ac.uk/pdbsum/3lfo PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lfo RCSB], [http://www.ebi.ac.uk/pdbsum/3lfo PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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> | 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> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Thermococcus celer]] | [[Category: Thermococcus celer]] | ||
[[Category: Chan, C H | [[Category: Chan, C H]] | ||
[[Category: Wong, K B | [[Category: Wong, K B]] | ||
[[Category: Globular protein]] | [[Category: Globular protein]] | ||
[[Category: L30e]] | [[Category: L30e]] | ||
[[Category: Ribosomal protein]] | [[Category: Ribosomal protein]] | ||
[[Category: Thermophilic]] | [[Category: Thermophilic]] | ||
Revision as of 02:23, 4 January 2015
Crystal structure of T. celer L30e E90A/R92A variantCrystal structure of T. celer L30e E90A/R92A variant
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMost 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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