PDBsum entry 3hsf

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protein links
Transcription regulation PDB id
Protein chain
92 a.a. *
* Residue conservation analysis
PDB id:
Name: Transcription regulation
Title: Heat shock transcription factor (hsf)
Structure: Heat shock transcription factor. Chain: a. Synonym: hsf. Engineered: yes. Mutation: yes
Source: Kluyveromyces lactis. Organism_taxid: 28985. Cell_line: bl21(de3). Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 30 models
Authors: F.F.Damberger,J.G.Pelton,C.Liu,H.Cho,C.J.Harrison, H.C.M.Nelson,D.E.Wemmer
Key ref:
F.F.Damberger et al. (1995). Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis. J Mol Biol, 254, 704-719. PubMed id: 7500344 DOI: 10.1006/jmbi.1995.0649
07-Aug-95     Release date:   14-Nov-95    
Supersedes: 2hsf
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P22121  (HSF_KLULA) -  Heat shock factor protein
677 a.a.
92 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of transcription, DNA-dependent   1 term 
  Biochemical function     sequence-specific DNA binding transcription factor activity     2 terms  


DOI no: 10.1006/jmbi.1995.0649 J Mol Biol 254:704-719 (1995)
PubMed id: 7500344  
Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis.
F.F.Damberger, J.G.Pelton, C.Liu, H.Cho, C.J.Harrison, H.C.Nelson, D.E.Wemmer.
The solution structure of the 92 residue (11 kDa) winged helix-turn-helix DNA-binding domain from the kluyveromyces lactis heat shock factor was refined using a total of 932 NOE, 35 phi, 25 chi 1, 5 chi 2 and 44 hydrogen bond restraints. The overall root-mean-square deviation for structured regions was 0.75(+/- 0.15) A. The three-helix bundle and four-stranded beta-sheet are well defined with rmsd of 0.53(+/- 0.10) A and 0.60(+/- 0.17) A, respectively. Helix H2 is underwound and bent near Pro45. The angle between helix H2 and the proposed recognition helix H3 is 96(+/- 6) degrees. Detailed comparisons are made with the X-ray structure of this protein as well as other structural studies on HSF. Overall, the results are consistent with the earlier studies. Differences are related to protein-protein interactions in the crystal and dynamics in solution. Backbone dynamics was investigated via 15N relaxation. The average R1, R2 and NOE values for residues in segments of secondary structure were 1.9(+/- 0.9) s-1, 7.8(+/- 0.9) s-1 and 0.81(+/- 0.05), respectively. The correlation time based on these data was 5.6(+/- 0.4) ns. Motional order parameters were calculated by fitting the relaxation data to one of three models. Low-order parameters were found for residues that comprise the turn between helices H2 and H3 (residues Lys49 to Phe53), and most strikingly, the 16 residue wing (residues Val68 to Arg83). These data are consistent with the lack of long-range NOEs identified in these regions. The data provide a basis for comparison with results of the protein-DNA complex. The relationship between structure and function is discussed.
  Selected figure(s)  
Figure 6.
Figure 6. Stereo view of heavy-atom coordinates for core residues with less than 20% solvent-accessible surface area. For a list of included residues see Table 1. The <rmsd> for this set of residues is 0.67(20.09) Å . Phe53 (arrow) is not defined by the data and shows two preferred conformations.
Figure 8.
Figure 8. Stereoview of the hydrophobic residues that form the turn between H2 and H3. Note the distortion in H2 between Leu44 and Phe48.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1995, 254, 704-719) copyright 1995.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19491106 K.Y.Chan-Schaminet, S.K.Baniwal, D.Bublak, L.Nover, and K.D.Scharf (2009).
Specific interaction between tomato HsfA1 and HsfA2 creates hetero-oligomeric superactivator complexes for synergistic activation of heat stress gene expression.
  J Biol Chem, 284, 20848-20857.  
11292844 M.P.Cicero, S.T.Hubl, C.J.Harrison, O.Littlefield, J.A.Hardy, and H.C.Nelson (2001).
The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity.
  Nucleic Acids Res, 29, 1715-1723.  
11511544 S.G.Ahn, P.C.Liu, K.Klyachko, R.I.Morimoto, and D.J.Thiele (2001).
The loop domain of heat shock transcription factor 1 dictates DNA-binding specificity and responses to heat stress.
  Genes Dev, 15, 2134-2145.  
  11305238 J.A.Hardy, and H.C.Nelson (2000).
Proline in alpha-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factor.
  Protein Sci, 9, 2128-2141.
PDB codes: 1fbq 1fbs 1fbu
9565750 J.P.Schneider, A.Lombardi, and W.F.DeGrado (1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
  Fold Des, 3, R29-R40.  
9241421 G.Patikoglou, and S.K.Burley (1997).
Eukaryotic transcription factor-DNA complexes.
  Annu Rev Biophys Biomol Struct, 26, 289-325.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.