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<StructureSection load='2hts' size='340' side='right'caption='[[2hts]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='2hts' size='340' side='right'caption='[[2hts]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_56498 Atcc 56498]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HTS FirstGlance]. <br>
<table><tr><td colspan='2'>[[2hts]] is a 1 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=2HTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HTS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</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=2hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hts OCA], [https://pdbe.org/2hts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hts RCSB], [https://www.ebi.ac.uk/pdbsum/2hts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hts ProSAT]</span></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=2hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hts OCA], [https://pdbe.org/2hts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hts RCSB], [https://www.ebi.ac.uk/pdbsum/2hts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hts ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2hts ConSurf].
</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=2hts ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha 2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.
Crystal structure of the DNA binding domain of the heat shock transcription factor.,Harrison CJ, Bohm AA, Nelson HC Science. 1994 Jan 14;263(5144):224-7. PMID:8284672<ref>PMID:8284672</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hts" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Heat shock factor|Heat shock factor]]
*[[Heat shock factor|Heat shock factor]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 56498]]
[[Category: Kluyveromyces lactis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Harrison, C]]
[[Category: Harrison C]]
[[Category: Nelson, H]]
[[Category: Nelson H]]
[[Category: Transcription factor]]

Latest revision as of 09:34, 14 February 2024

CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF THE HEAT SHOCK TRANSCRIPTION FACTOR

2hts, resolution 1.83Å

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