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PDBsum entry 2hsf
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protein links
Transcription regulation PDB id
2hsf

 

 

 

 

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Contents
Protein chain
92 a.a.
Superseded by: 3hsf
PDB id:
2hsf
Name: Transcription regulation
Title: Solution structure of the DNA-binding domain of heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy
Structure: Chain: null. Engineered: yes
Source: not given
NMR struc: 24 models
Authors: F.F.Damberger,J.G.Pelton,C.J.Harrison,H.C.M.Nelson, D.E.Wemmer
Key ref: F.F.Damberger et al. (1994). Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy. Protein Sci, 3, 1806-1821. PubMed id: 7849597 DOI: 10.1002/pro.5560031020
Date:
23-Jun-94     Release date:   15-Oct-94    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 92 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1002/pro.5560031020 Protein Sci 3:1806-1821 (1994)
PubMed id: 7849597  
 
 
Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.
F.F.Damberger, J.G.Pelton, C.J.Harrison, H.C.Nelson, D.E.Wemmer.
 
  ABSTRACT  
 
The solution structure of the 92-residue DNA-binding domain of the heat shock transcription factor from Kluyveromyces lactis has been determined using multidimensional NMR methods. Three-dimensional (3D) triple resonance, 1H-13C-13C-1H total correlation spectroscopy, and 15N-separated total correlation spectroscopy-heteronuclear multiple quantum correlation experiments were used along with various 2D spectra to make nearly complete assignments for the backbone and side-chain 1H, 15N, and 13C resonances. Five-hundred eighty-three NOE constraints identified in 3D 13C- and 15N-separated NOE spectroscopy (NOESY)-heteronuclear multiple quantum correlation spectra and a 4-dimensional 13C/13C-edited NOESY spectrum, along with 35 phi, 9 chi 1, and 30 hydrogen bond constraints, were used to calculate 30 structures by hybrid distance geometry/stimulated annealing protocol, of which 24 were used for structural comparison. The calculations revealed that a 3-helix bundle packs against a small 4-stranded antiparallel beta-sheet. The backbone RMS deviation (RMSD) for the family of structures was 1.03 +/- 0.19 A with respect to the average structure. The topology is analogous to that of the C-terminal domain of the catabolite gene activator protein and appears to be in the helix-turn-helix family of DNA-binding proteins. The overall fold determined by the NMR data is consistent with recent crystallographic work on this domain (Harrison CJ, Bohm AA, Nelson HCM, 1994, Science 263:224) as evidenced by RMSD between backbone atoms in the NMR and X-ray structures of 1.77 +/- 0.20 A. Several differences were identified some of which may be due to protein-protein interactions in the crystal.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21082705 J.Lin, T.Zhou, and J.Wang (2011).
Solution structure of the human HSPC280 protein.
  Protein Sci, 20, 216-223.
PDB code: 2l2o
20499070 H.Xin, H.Zhang, L.Chen, X.Li, Q.Lian, X.Yuan, X.Hu, L.Cao, X.He, and M.Yi (2010).
Cloning and characterization of HsfA2 from Lily (Lilium longiflorum).
  Plant Cell Rep, 29, 875-885.  
20628411 M.Akerfelt, R.I.Morimoto, and L.Sistonen (2010).
Heat shock factors: integrators of cell stress, development and lifespan.
  Nat Rev Mol Cell Biol, 11, 545-555.  
19190998 Y.Hou, and J.Zou (2009).
Delivery of HSF1(+) protein using HIV-1 TAT protein transduction domain.
  Mol Biol Rep, 36, 2271-2277.  
18270585 S.Bandhakavi, H.Xie, B.O'Callaghan, H.Sakurai, D.H.Kim, and T.J.Griffin (2008).
Hsf1 activation inhibits rapamycin resistance and TOR signaling in yeast revealed by combined proteomic and genetic analysis.
  PLoS ONE, 3, e1598.  
14978306 P.Gutiérrez, M.J.Osborne, N.Siddiqui, J.F.Trempe, C.Arrowsmith, and K.Gehring (2004).
Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: implications for translation initiation.
  Protein Sci, 13, 659-667.
PDB code: 1nee
15625403 S.K.Baniwal, K.Bharti, K.Y.Chan, M.Fauth, A.Ganguli, S.Kotak, S.K.Mishra, L.Nover, M.Port, K.D.Scharf, J.Tripp, C.Weber, D.Zielinski, and P.von Koskull-Döring (2004).
Heat stress response in plants: a complex game with chaperones and more than twenty heat stress transcription factors.
  J Biosci, 29, 471-487.  
12032317 U.Yamanouchi, M.Yano, H.Lin, M.Ashikari, and K.Yamada (2002).
A rice spotted leaf gene, Spl7, encodes a heat stress transcription factor protein.
  Proc Natl Acad Sci U S A, 99, 7530-7535.  
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.  
  10888672 D.C.Raitt, A.L.Johnson, A.M.Erkine, K.Makino, B.Morgan, D.S.Gross, and L.H.Johnston (2000).
The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsf1 in vivo and is required for the induction of heat shock genes by oxidative stress.
  Mol Biol Cell, 11, 2335-2347.  
  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
  10794414 M.A.Keniry, H.A.Berthon, J.Y.Yang, C.S.Miles, and N.E.Dixon (2000).
NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
  Protein Sci, 9, 721-733.
PDB code: 1du2
9659911 G.Mizuguchi, T.Tsukiyama, J.Wisniewski, and C.Wu (1997).
Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin.
  Mol Cell, 1, 141-150.  
  8745404 H.S.Cho, C.W.Liu, F.F.Damberger, J.G.Pelton, H.C.Nelson, and D.E.Wemmer (1996).
Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
  Protein Sci, 5, 262-269.  
8665913 J.Schultheiss, O.Kunert, U.Gase, K.D.Scharf, L.Nover, and H.Rüterjans (1996).
Solution structure of the DNA-binding domain of the tomato heat-stress transcription factor HSF24.
  Eur J Biochem, 236, 911-921.  
  8598195 L.W.Donaldson, J.M.Petersen, B.J.Graves, and L.P.McIntosh (1996).
Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif.
  EMBO J, 15, 125-134.
PDB codes: 1etc 1etd
  7651423 F.A.Torres, and J.J.Bonner (1995).
Genetic identification of the site of DNA contact in the yeast heat shock transcription factor.
  Mol Cell Biol, 15, 5063-5070.  
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 code is shown on the right.

 

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