2hts

<StructureSection load='2hts' size='340' side='right' caption='[[2hts]], [[Resolution|resolution]] 1.83&Aring;' scene=''>

<table><tr><td colspan='2'>[[2hts]] is a 1 chain structure with 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=2HTS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HTS FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hts OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hts RCSB], [http://www.ebi.ac.uk/pdbsum/2hts PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/2hts_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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== References ==

<references/>

[[Category: Harrison, C]]

[[Category: Nelson, H]]

[[Category: Transcription factor]]