1HIO

HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY

Summary for 1HIO

• Entry DOI: 10.2210/pdb1hio/pdb
• Descriptor: HISTONE H2A, HISTONE H2B, HISTONE H3, ... (4 entities in total)
• Functional Keywords: histone, chromosomal protein, nucleosome core
• Biological source: Gallus gallus (chicken); More
• Cellular location: Nucleus: P02263 P84229 P62801
• Total number of polymer chains: 4
• Total formula weight: 39656.09

Authors

Arents, G.,Moudrianakis, E.N. (deposition date: 1991-09-19, release date: 1998-11-25, Last modification date: 2024-02-07)

Primary citation

Arents, 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

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)