Crystal structure of globular domain of histone H5 and its implications for nucleosome binding.
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.
Biology Department, Brookhaven National Laboratory, Upton, New York 11973.
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V
Ramakrishnan
J T
JT
Finch
V
V
Graziano
P L
PL
Lee
R M
RM
Sweet
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000378:metabolism*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014961:X-Ray Diffraction / Q000379:methods
D002373:Cyclic AMP Receptor Protein; D004268:DNA-Binding Proteins; D006657:Histones; D009707:Nucleosomes; D011994:Recombinant Proteins; D004247:DNA