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New page: left|200px<br /><applet load="1hkt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hkt" /> '''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN...
 
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[[Image:1hkt.jpg|left|200px]]<br /><applet load="1hkt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hkt" />
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR==
The solution structure of the DNA-binding domain of the Drosophila heat, shock transcription factor, as determined by multidimensional multinuclear, NMR, resembles that of the helix-turn-helix class of DNA-binding proteins., The domain comprises a four-stranded antiparallel beta-sheet, packed, against a three-helix bundle. The second helix is significantly distorted, and is separated from the third helix by an extended turn which is subject, to conformational averaging on an intermediate time scale. Helix 3 forms a, classical amphipathic helix with polar and charged residues exposed to the, solvent. Upon titration with DNA, resonance shifts in the backbone and Asn, and Gln side-chain amides indicate that helix 3 acts as the recognition, helix of the heat shock transcription factor.
<StructureSection load='1hkt' size='340' side='right'caption='[[1hkt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hkt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HKT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hkt OCA], [https://pdbe.org/1hkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hkt RCSB], [https://www.ebi.ac.uk/pdbsum/1hkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hkt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSF_DROME HSF_DROME] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
== 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/hk/1hkt_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=1hkt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of the DNA-binding domain of the Drosophila heat shock transcription factor, as determined by multidimensional multinuclear NMR, resembles that of the helix-turn-helix class of DNA-binding proteins. The domain comprises a four-stranded antiparallel beta-sheet, packed against a three-helix bundle. The second helix is significantly distorted and is separated from the third helix by an extended turn which is subject to conformational averaging on an intermediate time scale. Helix 3 forms a classical amphipathic helix with polar and charged residues exposed to the solvent. Upon titration with DNA, resonance shifts in the backbone and Asn and Gln side-chain amides indicate that helix 3 acts as the recognition helix of the heat shock transcription factor.


==About this Structure==
Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor.,Vuister GW, Kim SJ, Orosz A, Marquardt J, Wu C, Bax A Nat Struct Biol. 1994 Sep;1(9):605-14. PMID:7634100<ref>PMID:7634100</ref>
1HKT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HKT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor., Vuister GW, Kim SJ, Orosz A, Marquardt J, Wu C, Bax A, Nat Struct Biol. 1994 Sep;1(9):605-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7634100 7634100]
</div>
<div class="pdbe-citations 1hkt" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Heat shock factor|Heat shock factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bax, A.]]
[[Category: Bax A]]
[[Category: Kim, S.J.]]
[[Category: Kim S-J]]
[[Category: Marquardt, J.L.]]
[[Category: Marquardt JL]]
[[Category: Orosz, A.]]
[[Category: Orosz A]]
[[Category: Vuister, G.W.]]
[[Category: Vuister GW]]
[[Category: Wu, C.]]
[[Category: Wu C]]
[[Category: transcription regulation]]
 
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Latest revision as of 08:32, 22 May 2024

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR

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