1fbq: Difference between revisions

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New page: left|200px<br /><applet load="1fbq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fbq, resolution 2.00Å" /> '''HEAT SHOCK TRANSCRIP...
 
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[[Image:1fbq.jpg|left|200px]]<br /><applet load="1fbq" size="450" color="white" frame="true" align="right" spinBox="true"
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'''HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATION'''<br />


==Overview==
==HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATION==
The DNA-binding domain of the yeast heat shock transcription factor (HSF), contains a strictly conserved proline that is at the center of a kink. To, define the role of this conserved proline-centered kink, we replaced the, proline with a number of other residues. These substitutions did not, diminish the ability of the full-length protein to support growth of yeast, or to activate transcription, suggesting that the proline at the center of, the kink is not conserved for function. The stability of the isolated, mutant DNA-binding domains was unaltered from the wild-type, so the, proline is not conserved to maintain the stability of the protein. The, crystal structures of two of the mutant DNA-binding domains revealed that, the helices in the mutant proteins were still kinked after substitution of, the proline, suggesting that the proline does not cause the alpha-helical, kink. So why are prolines conserved in this and the majority of other, kinked alpha-helices if not for structure, function, or stability? The, mutant DNA-binding domains are less soluble than wild-type when, overexpressed. In addition, the folding kinetics, as measured by, stopped-flow fluorescence, is faster for the mutant proteins. These two, results support the premise that the presence of the proline is critical, for the folding pathway of HSF's DNA-binding domain. The finding may also, be more general and explain why kinked helices maintain their prolines.
<StructureSection load='1fbq' size='340' side='right'caption='[[1fbq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fbq]] 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=1FBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBQ 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]] 2&#8491;</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=1fbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fbq OCA], [https://pdbe.org/1fbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fbq RCSB], [https://www.ebi.ac.uk/pdbsum/1fbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fbq 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/fb/1fbq_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=1fbq ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FBQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FBQ OCA].
*[[Heat shock factor|Heat shock factor]]
 
__TOC__
==Reference==
</StructureSection>
Proline in alpha-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factor., Hardy JA, Nelson HC, Protein Sci. 2000 Nov;9(11):2128-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11305238 11305238]
[[Category: Kluyveromyces lactis]]
[[Category: Kluyveromyces lactis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hardy, J.A.]]
[[Category: Hardy JA]]
[[Category: Nelson, H.C.M.]]
[[Category: Nelson HCM]]
[[Category: helical bulge]]
[[Category: helical kink]]
[[Category: helix-turn-helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:48:01 2007''

Latest revision as of 10:12, 7 February 2024

HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATIONHEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATION

Structural highlights

1fbq is a 2 chain structure with sequence from Kluyveromyces lactis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1fbq, resolution 2.00Å

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