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5d60

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Revision as of 10:23, 21 June 2023

Structure of Chaetomium thermophilum Skn7 coiled-coil domain, crystal form III

Structural highlights

5d60 is a 4 chain structure with sequence from Chaetomium thermophilum. 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

SKN7_CHATD Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes.[UniProtKB:P38889]

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^[1]

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

References

↑ 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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d60"

@@ Line 3: / Line 3: @@
 <StructureSection load='5d60' size='340' side='right'caption='[[5d60]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5d60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D60 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5d60]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D60 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0048700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=209285 CBS 144.50])</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=5d60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d60 OCA], [https://pdbe.org/5d60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d60 RCSB], [https://www.ebi.ac.uk/pdbsum/5d60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d60 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=5d60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d60 OCA], [http://pdbe.org/5d60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d60 RCSB], [http://www.ebi.ac.uk/pdbsum/5d60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d60 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SKN7_CHATD SKN7_CHATD] Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes.[UniProtKB:P38889]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Cbs 144 50]]
+[[Category: Chaetomium thermophilum]]
 [[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: Coiled-coil]]
-[[Category: Transcription]]

5d60

From Proteopedia

Revision as of 10:23, 21 June 2023

Structure of Chaetomium thermophilum Skn7 coiled-coil domain, crystal form III

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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