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The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
Open accessAbstract
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.
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Metadata
- Authors
- Arents, G., Burlingame, R. W., Wang, B. C., Love, W. E., & Moudrianakis, E. N.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1991-11-15
- Volume
- 88
- Issue
- 22
- Pages
- 10148-10152
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2010048885
- Cited by
- 759
- References
- 0
- FWCI
- 6.34
- Type
- journal article
- Language
- en
- Open access
- green
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