View source for 2wqg


==SAP domain from Tho1: L31W (fluorophore) mutant==
<StructureSection load='2wqg' size='340' side='right'caption='[[2wqg]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQG FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h1j|1h1j]]</div></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=2wqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqg OCA], [https://pdbe.org/2wqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wqg RCSB], [https://www.ebi.ac.uk/pdbsum/2wqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wqg ProSAT]</span></td></tr>
</table>
== 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/wq/2wqg_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=2wqg ConSurf].
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== Publication Abstract from PubMed ==
The SAP domain from the Saccharomyces cerevisiae THO1 protein contains a hydrophobic core and just two alpha-helices. It could provide a system for studying protein folding that bridges the gap between studies on isolated helices and those on larger protein domains. We have engineered the SAP domain for protein folding studies by inserting a tryptophan residue into the hydrophobic core (L31W) and solved its structure. The helical regions had a backbone root mean-squared deviation of 0.9 A from those of wild type. The mutation L31W destabilised wild type by 0.8 +/- 0.1 kcal mol(-1). The mutant folded in a reversible, apparent two-state manner with a microscopic folding rate constant of around 3700 s(-1) and is suitable for extended studies of folding.

Engineering a two-helix bundle protein for folding studies.,Dodson CA, Ferguson N, Rutherford TJ, Johnson CM, Fersht AR Protein Eng Des Sel. 2010 May;23(5):357-64. Epub 2010 Feb 3. PMID:20130106<ref>PMID:20130106</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2wqg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Dodson, C A]]
[[Category: Ferguson, N]]
[[Category: Fersht, A R]]
[[Category: Johnson, C M]]
[[Category: Rutherford, T J]]
[[Category: Unknown function]]