1fbs: Difference between revisions

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 <StructureSection load='1fbs' size='340' side='right'caption='[[1fbs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fbs]] is a 2 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=1FBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fbs]] 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=1FBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBS FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fbq|1fbq]], [[1fbu|1fbu]], [[2hts|2hts]]</div></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]] 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=1fbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fbs OCA], [https://pdbe.org/1fbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fbs RCSB], [https://www.ebi.ac.uk/pdbsum/1fbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fbs 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.
+[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]]
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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=1fbs ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:11305238<ref>PMID:11305238</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1fbs" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Heat shock factor|Heat shock factor]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 56498]]
+[[Category: Kluyveromyces lactis]]
 [[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]]
-[[Category: Transcription]]