1hio
From Proteopedia
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[[Image:1hio.gif|left|200px]] | [[Image:1hio.gif|left|200px]] | ||
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'''HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY''' | '''HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY''' | ||
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[[Category: Arents, G.]] | [[Category: Arents, G.]] | ||
[[Category: Moudrianakis, E N.]] | [[Category: Moudrianakis, E N.]] | ||
- | [[Category: | + | [[Category: Chromosomal protein]] |
- | [[Category: | + | [[Category: Histone]] |
- | [[Category: | + | [[Category: Nucleosome core]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:53:02 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:53, 2 May 2008
HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY
Overview
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.
About this Structure
1HIO is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
Reference
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix., Arents G, Burlingame RW, Wang BC, Love WE, Moudrianakis EN, Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10148-52. PMID:1946434 Page seeded by OCA on Fri May 2 18:53:02 2008