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2HIO

HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN

Summary for 2HIO
Entry DOI10.2210/pdb2hio/pdb
Related1HIO
DescriptorPROTEIN (HISTONE H2A), PROTEIN (HISTONE H2B), PROTEIN (HISTONE H3), ... (4 entities in total)
Functional Keywordshistone, chromosomal protein, structural protein, dna binding protein
Biological sourceGallus gallus (chicken)
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Cellular locationNucleus: P02263 P84229 P62801
Total number of polymer chains4
Total formula weight54547.81
Authors
Arents, G.,Moudrianakis, E.N. (deposition date: 1999-06-15, release date: 2000-01-12, Last modification date: 2023-12-27)
Primary citationArents, G.,Burlingame, R.W.,Wang, B.C.,Love, W.E.,Moudrianakis, E.N.
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
Proc.Natl.Acad.Sci.USA, 88:10148-10152, 1991
Cited by
PubMed Abstract: The structure of the octameric histone core of the nucleosome has been determined by x-ray crystallography to a resolution of 3.1 A. The histone octamer is a tripartite assembly in which a centrally located (H3-H4)2 tetramer is flanked by two H2A-H2B dimers. It has a complex outer surface; depending on the perspective, the structure appears as a wedge or as a flat disk. The disk represents the planar projection of a left-handed proteinaceous superhelix with approximately 28 A pitch. The diameter of the particle is 65 A and the length is 60 A at its maximum and approximately 10 A at its minimum extension; these dimensions are in agreement with those reported earlier by Klug et al. [Klug, A., Rhodes, D., Smith, J., Finch, J. T. & Thomas, J. O. (1980) Nature (London) 287, 509-516]. The folded histone chains are elongated rather than globular and are assembled in a characteristic "handshake" motif. The individual polypeptides share a common central structural element of the helix-loop-helix type, which we name the histone fold.
PubMed: 1946434
DOI: 10.1073/pnas.88.22.10148
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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