A model for histone H5-DNA interaction: simultaneous minor and major groove binding.
Using the tertiary structure of the globular domain of H5 (GH5) and based on an alternative sequence homology between GH5 and DNA-binding proteins containing the helix-turn-helix motif, a model for H5-DNA interaction is proposed. From molecular graphics it follows that helix II recognizes the major groove of the DNA, as does the second helix of the helix-turn-helix motif, while helix III makes minor groove contacts, in agreement with the hypothesis of Turnell et al. (FEBS letters 232, 263-268). In the resulting model GH5 makes contact with a full turn of DNA.
Segers
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A
Vrije Universiteit Brussel, Institut voor Moleculaire Biologie, St. Genesius-Rode, Belgium.
Wyns
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Lasters
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I
D000595:Amino Acid Sequence; D002373:Cyclic AMP Receptor Protein / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D002373:Cyclic AMP Receptor Protein; D006657:Histones; D004247:DNA