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5d5u

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Revision as of 10:22, 21 June 2023

Crystal structure of human Hsf1 with HSE DNA

Structural highlights

5d5u is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSF1_HUMAN 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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Heat-shock transcription factor 1 (HSF1) has a central role in mediating the protective response to protein conformational stresses in eukaryotes. HSF1 consists of an N-terminal DNA-binding domain (DBD), a coiled-coil oligomerization domain, a regulatory domain and a transactivation domain. Upon stress, HSF1 trimerizes via its coiled-coil domain and binds to the promoters of heat shock protein-encoding genes. Here, we present cocrystal structures of the human HSF1 DBD in complex with cognate DNA. A comparative analysis of the HSF1 paralog Skn7 from Chaetomium thermophilum showed that single amino acid changes in the DBD can switch DNA binding specificity, thus revealing the structural basis for the interaction of HSF1 with cognate DNA. We used a crystal structure of the coiled-coil domain of C. thermophilum Skn7 to develop a model of the active human HSF1 trimer in which HSF1 embraces the heat-shock-element DNA.

Structure of human heat-shock transcription factor 1 in complex with DNA.,Neudegger T, Verghese J, Hayer-Hartl M, Hartl FU, Bracher A Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3149. PMID:26727489^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Holmberg CI, Hietakangas V, Mikhailov A, Rantanen JO, Kallio M, Meinander A, Hellman J, Morrice N, MacKintosh C, Morimoto RI, Eriksson JE, Sistonen L. Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1. EMBO J. 2001 Jul 16;20(14):3800-10. PMID:11447121 doi:http://dx.doi.org/10.1093/emboj/20.14.3800
↑ Knauf U, Newton EM, Kyriakis J, Kingston RE. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 1996 Nov 1;10(21):2782-93. PMID:8946918
↑ Kline MP, Morimoto RI. Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Mol Cell Biol. 1997 Apr;17(4):2107-15. PMID:9121459
↑ Xia W, Guo Y, Vilaboa N, Zuo J, Voellmy R. Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo. J Biol Chem. 1998 Apr 10;273(15):8749-55. PMID:9535852
↑ Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, Toft DO, Smith DF, Voellmy R. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J Biol Chem. 2001 Dec 7;276(49):45791-9. Epub 2001 Oct 2. PMID:11583998 doi:http://dx.doi.org/10.1074/jbc.M105931200
↑ Soncin F, Zhang X, Chu B, Wang X, Asea A, Ann Stevenson M, Sacks DB, Calderwood SK. Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem Biophys Res Commun. 2003 Apr 4;303(2):700-6. PMID:12659875
↑ Hietakangas V, Ahlskog JK, Jakobsson AM, Hellesuo M, Sahlberg NM, Holmberg CI, Mikhailov A, Palvimo JJ, Pirkkala L, Sistonen L. Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol Cell Biol. 2003 Apr;23(8):2953-68. PMID:12665592
↑ Wang X, Khaleque MA, Zhao MJ, Zhong R, Gaestel M, Calderwood SK. Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J Biol Chem. 2006 Jan 13;281(2):782-91. Epub 2005 Nov 8. PMID:16278218 doi:M505822200
↑ Neudegger T, Verghese J, Hayer-Hartl M, Hartl FU, Bracher A. Structure of human heat-shock transcription factor 1 in complex with DNA. Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3149. PMID:26727489 doi:http://dx.doi.org/10.1038/nsmb.3149

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d5u"

@@ Line 3: / Line 3: @@
 <StructureSection load='5d5u' size='340' side='right'caption='[[5d5u]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5d5u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D5U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5d5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D5U FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSF1, HSTF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=5d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5u OCA], [https://pdbe.org/5d5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d5u RCSB], [https://www.ebi.ac.uk/pdbsum/5d5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5u ProSAT]</span></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=5d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5u OCA], [http://pdbe.org/5d5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d5u RCSB], [http://www.ebi.ac.uk/pdbsum/5d5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HSF1_HUMAN HSF1_HUMAN]] 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.<ref>PMID:11447121</ref> <ref>PMID:8946918</ref> <ref>PMID:9121459</ref> <ref>PMID:9535852</ref> <ref>PMID:11583998</ref> <ref>PMID:12659875</ref> <ref>PMID:12665592</ref> <ref>PMID:16278218</ref>
+[https://www.uniprot.org/uniprot/HSF1_HUMAN HSF1_HUMAN] 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.<ref>PMID:11447121</ref> <ref>PMID:8946918</ref> <ref>PMID:9121459</ref> <ref>PMID:9535852</ref> <ref>PMID:11583998</ref> <ref>PMID:12659875</ref> <ref>PMID:12665592</ref> <ref>PMID:16278218</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bracher, A]]
+[[Category: Bracher A]]
-[[Category: Hartl, F U]]
+[[Category: Hartl FU]]
-[[Category: Hayer-Hartl, M]]
+[[Category: Hayer-Hartl M]]
-[[Category: Neudegger, T]]
+[[Category: Neudegger T]]
-[[Category: Verghese, J]]
+[[Category: Verghese J]]
-[[Category: Double helix]]
-[[Category: Helix-turn-helix]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription-dna complex]]

5d5u

From Proteopedia

Revision as of 10:22, 21 June 2023

Crystal structure of human Hsf1 with HSE DNA

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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