3lfo: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3lfo.png|left|200px]]
-<!--
+==Crystal structure of T. celer L30e E90A/R92A variant==
-The line below this paragraph, containing "STRUCTURE_3lfo", creates the "Structure Box" on the page.
+<StructureSection load='3lfo' size='340' side='right'caption='[[3lfo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3lfo]] is a 1 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=3LFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LFO FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lfo OCA], [https://pdbe.org/3lfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lfo RCSB], [https://www.ebi.ac.uk/pdbsum/3lfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lfo ProSAT]</span></td></tr>
-{{STRUCTURE_3lfo|  PDB=3lfo  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lf/3lfo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lfo ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Crystal structure of T. celer L30e E90A/R92A variant===
+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 MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_21720566}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3lfo" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21720566 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21720566}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[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].
-==Reference==
-<ref group="xtra">PMID:021720566</ref><references group="xtra"/>
 [[Category: Thermococcus celer]]
-[[Category: Chan, C H.]]
+[[Category: Chan CH]]
-[[Category: Wong, K B.]]
+[[Category: Wong KB]]
-[[Category: Globular protein]]
-[[Category: L30e]]
-[[Category: Ribosomal protein]]
-[[Category: Thermophilic]]