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PDBsum entry 3hsf
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Transcription regulation
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PDB id
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3hsf
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References listed in PDB file
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Key reference
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Title
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Refined solution structure and dynamics of the DNA-Binding domain of the heat shock factor from kluyveromyces lactis.
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Authors
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F.F.Damberger,
J.G.Pelton,
C.Liu,
H.Cho,
C.J.Harrison,
H.C.Nelson,
D.E.Wemmer.
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Ref.
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J Mol Biol, 1995,
254,
704-719.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
96%.
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1995,
254,
704-719)
copyright 1995.
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Secondary reference #1
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Title
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Crystal structure of the DNA binding domain of the heat shock transcription factor.
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Authors
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C.J.Harrison,
A.A.Bohm,
H.C.Nelson.
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Ref.
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Science, 1994,
263,
224-227.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Solution structure of the DNA-Binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.
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Authors
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F.F.Damberger,
J.G.Pelton,
C.J.Harrison,
H.C.Nelson,
D.E.Wemmer.
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Ref.
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Protein Sci, 1994,
3,
1806-1821.
[DOI no: ]
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PubMed id
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