PDBsum entry 3hsf

Transcription regulation

PDB id: 3hsf

Contents

Protein chain

92 a.a. *

* Residue conservation analysis

PDB id:

3hsf

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

Date:

07-Aug-95 Release date: 14-Nov-95

Supersedes:

2hsf

Protein chain

P22121  (HSF_KLULA) -  Heat shock transcription factor from Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)

Seq: 677 a.a.

Struc: 92 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

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.

ABSTRACT

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.