1w40

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{{Seed}}
 
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[[Image:1w40.png|left|200px]]
 
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==T. celer L30e K9A variant==
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The line below this paragraph, containing "STRUCTURE_1w40", creates the "Structure Box" on the page.
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<StructureSection load='1w40' size='340' side='right'caption='[[1w40]], [[Resolution|resolution]] 2.03&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'>[[1w40]] 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=1W40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W40 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.03&#8491;</td></tr>
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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=1w40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w40 OCA], [https://pdbe.org/1w40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w40 RCSB], [https://www.ebi.ac.uk/pdbsum/1w40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w40 ProSAT]</span></td></tr>
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{{STRUCTURE_1w40| PDB=1w40 | SCENE= }}
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/1w40_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1w40 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The origin of reduced heat capacity change of unfolding (DeltaC(p)) commonly observed in thermophilic proteins is controversial. The established theory that DeltaC(p) is correlated with change of solvent-accessible surface area cannot account for the large differences in DeltaC(p) observed for thermophilic and mesophilic homologous proteins, which are very similar in structures. We have determined the protein stability curves, which describe the temperature dependency of the free energy change of unfolding, for a thermophilic ribosomal protein L30e from Thermococcus celer, and its mesophilic homologue from yeast. Values of DeltaC(p), obtained by fitting the free energy change of unfolding to the Gibbs-Helmholtz equation, were 5.3 kJ mol(-1) K(-1) and 10.5 kJ mol(-1) K(-1) for T.celer and yeast L30e, respectively. We have created six charge-to-neutral mutants of T.celer L30e. Removal of charges at Glu6, Lys9, and Arg92 decreased the melting temperatures of T.celer L30e by approximately 3-9 degrees C, and the differences in melting temperatures were smaller with increasing concentration of salt. These results suggest that these mutations destabilize T.celer L30e by disrupting favorable electrostatic interactions. To determine whether electrostatic interactions contribute to the reduced DeltaC(p) of the thermophilic protein, we have determined DeltaC(p) for wild-type and mutant T.celer L30e by Gibbs-Helmholtz and by van't Hoff analyses. A concomitant increase in DeltaC(p) was observed for those charge-to-neutral mutants that destabilize T.celer L30e by removing favorable electrostatic interactions. The crystal structures of K9A, E90A, and R92A, were determined, and no structural change was observed. Taken together, our results support the conclusion that electrostatic interactions contribute to the reduced DeltaC(p) of T.celer L30e.
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===T. CELER L30E K9A VARIANT===
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Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e.,Lee CF, Allen MD, Bycroft M, Wong KB J Mol Biol. 2005 Apr 29;348(2):419-31. PMID:15811378<ref>PMID:15811378</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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The line below this paragraph, {{ABSTRACT_PUBMED_15811378}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1w40" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15811378 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15811378}}
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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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1W40 is a 1 chain structure of 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=1W40 OCA].
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==Reference==
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<ref group="xtra">PMID:15811378</ref><references group="xtra"/>
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[[Category: Thermococcus celer]]
[[Category: Thermococcus celer]]
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[[Category: Allen, M D.]]
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[[Category: Allen MD]]
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[[Category: Bycroft, M.]]
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[[Category: Bycroft M]]
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[[Category: Chan, S H.]]
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[[Category: Chan SH]]
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[[Category: Lee, C F.]]
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[[Category: Lee CF]]
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[[Category: Lee, K M.]]
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[[Category: Lee KM]]
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[[Category: Wong, K B.]]
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[[Category: Wong KB]]
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[[Category: Electrostatic interaction]]
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[[Category: Protein engineering]]
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[[Category: Ribosomal protein]]
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[[Category: Thermostability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:10:12 2009''
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Current revision

T. celer L30e K9A variant

PDB ID 1w40

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