Crystal structure of globular domain of histone H5 and its implications for nucleosome binding

• Published in: Nature (London) Vol. 362; no. 6417; pp. 219 - 223
• Main Authors: Ramakrishnan, V, Finch, J. T, Graziano, V, Lee, P. L, Sweet, R. M
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 18-03-1993; Nature Publishing Group
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Biology; Cloning, Molecular; Crystals; Cyclic AMP Receptor Protein - chemistry; Deoxyribonucleic acid; DNA; DNA - metabolism; DNA-Binding Proteins - chemistry; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Histones - chemistry; Histones - genetics; Histones - metabolism; Holoproteins; Magnetic Resonance Spectroscopy - methods; Models, Molecular; Molecular Sequence Data; Nuclear proteins; Nucleosomes - metabolism; Protein Structure, Secondary; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; X-Ray Diffraction - methods; Histone H5; Chromatin; Domain structure; Molecular structure; DNA; Nucleosome; Molecular interaction; Models; Structure function relationship; Comparative study; Crystalline structure
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/362219a0

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.