1hio: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hio OCA], [http://www.ebi.ac.uk/pdbsum/1hio PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hio RCSB]</span> | |||
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[[Category: nucleosome core]] | [[Category: nucleosome core]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:39 2008'' | ||
Revision as of 21:05, 30 March 2008
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| , resolution 3.10Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY
OverviewOverview
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 StructureAbout this Structure
1HIO is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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
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