Abstract
The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 A resolution by multiwavelength anomalous diffraction on crystals of the selenomethionyl protein. The structure shows a striking similarity to the DNA-binding domain of the catabolite gene activator protein CAP, thereby providing a possible model for the binding of GH5 to DNA.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Cloning, Molecular
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Cyclic AMP Receptor Protein / chemistry
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DNA / metabolism
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DNA-Binding Proteins / chemistry
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Escherichia coli / genetics
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Histones / chemistry*
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Histones / genetics
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Histones / metabolism*
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Magnetic Resonance Spectroscopy / methods
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Models, Molecular
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Molecular Sequence Data
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Nucleosomes / metabolism*
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Protein Structure, Secondary*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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X-Ray Diffraction / methods
Substances
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Cyclic AMP Receptor Protein
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DNA-Binding Proteins
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Histones
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Nucleosomes
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Recombinant Proteins
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DNA