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[[Image:3hts.jpg|left|200px]]
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{{STRUCTURE_3hts|  PDB=3hts  |  SCENE=  }}
'''HEAT SHOCK TRANSCRIPTION FACTOR/DNA COMPLEX'''


==HEAT SHOCK TRANSCRIPTION FACTOR/DNA COMPLEX==
<StructureSection load='3hts' size='340' side='right'caption='[[3hts]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3hts]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HTS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hts OCA], [https://pdbe.org/3hts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hts RCSB], [https://www.ebi.ac.uk/pdbsum/3hts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hts ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSF_KLULA HSF_KLULA] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. Also required for growth at normal temperatures.
== 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/ht/3hts_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=3hts ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 1.75 A crystal structure of the Kluyveromyces lactis heat shock transcription factor (HSF) DNA-binding domain (DBD) complexed with DNA reveals a protein-DNA interface with few direct major groove contacts and a number of phosphate backbone contacts that are primarily water-mediated interactions. The DBD, a 'winged' helix-turn-helix protein, displays a novel mode of binding in that the 'wing' does not contact DNA like all others of that class. Instead, the monomeric DBD, which crystallized as a symmetric dimer to a pair of nGAAn inverted repeats, uses the 'wing' to form part of the protein-protein contacts. This dimer interface is likely important for increasing the DNA-binding specificity and affinity of the trimeric form of HSF, as well as for increasing cooperativity between adjacent trimers.


==Overview==
A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal.,Littlefield O, Nelson HC Nat Struct Biol. 1999 May;6(5):464-70. PMID:10331875<ref>PMID:10331875</ref>
The 1.75 A crystal structure of the Kluyveromyces lactis heat shock transcription factor (HSF) DNA-binding domain (DBD) complexed with DNA reveals a protein-DNA interface with few direct major groove contacts and a number of phosphate backbone contacts that are primarily water-mediated interactions. The DBD, a 'winged' helix-turn-helix protein, displays a novel mode of binding in that the 'wing' does not contact DNA like all others of that class. Instead, the monomeric DBD, which crystallized as a symmetric dimer to a pair of nGAAn inverted repeats, uses the 'wing' to form part of the protein-protein contacts. This dimer interface is likely important for increasing the DNA-binding specificity and affinity of the trimeric form of HSF, as well as for increasing cooperativity between adjacent trimers.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3HTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HTS OCA].
</div>
<div class="pdbe-citations 3hts" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal., Littlefield O, Nelson HC, Nat Struct Biol. 1999 May;6(5):464-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10331875 10331875]
*[[Heat shock factor|Heat shock factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kluyveromyces lactis]]
[[Category: Kluyveromyces lactis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Littlefield, O.]]
[[Category: Littlefield O]]
[[Category: Nelson, H C.M.]]
[[Category: Nelson HCM]]
[[Category: Dna-binding protein]]
[[Category: Transcription regulation]]
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Retrieved from "https://proteopedia.org/3hts"