3hsf

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Revision as of 20:40, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="3hsf" size="450" color="white" frame="true" align="right" spinBox="true" caption="3hsf" /> '''HEAT SHOCK TRANSCRIPTION FACTOR (HSF)'''<br ...)
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3hsf

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HEAT SHOCK TRANSCRIPTION FACTOR (HSF)

OverviewOverview

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.

About this StructureAbout this Structure

3HSF is a Single protein structure of sequence from Kluyveromyces lactis. This structure superseeds the now removed PDB entry 2HSF. Full crystallographic information is available from OCA.

ReferenceReference

Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis., Damberger FF, Pelton JG, Liu C, Cho H, Harrison CJ, Nelson HC, Wemmer DE, J Mol Biol. 1995 Dec 8;254(4):704-19. PMID:7500344

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