Publication Date:
1985-05-03
Description:
The structure of the (H2A-H2B-H3-H4)2 histone octamer has been determined by means of x-ray crystallographic techniques at a resolution of 3.3 angstroms. The octamer is a prolate ellipsoid 110 angstroms long and 65 to 70 angstroms in diameter, and its general shape is that of a rugby ball. The size and shape are radically different from those determined in earlier studies. The most striking feature of the histone octamer is its tripartite organization, that is, a central (H3-H4)2 tetramer flanked by two H2A-H2B dimers. The DNA helix, placed around the octamer in a path suggested by the features on the surface of the protein, appears like a spring holding the H2A-H2B dimers at either end of the (H3-H4)2 tetramer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burlingame, R W -- Love, W E -- Wang, B C -- Hamlin, R -- Nguyen, H X -- Moudrianakis, E N -- New York, N.Y. -- Science. 1985 May 3;228(4699):546-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3983639" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Chickens
;
Chromatin/ultrastructure
;
DNA/metabolism
;
*Histones/metabolism
;
Models, Chemical
;
Nucleosomes/*ultrastructure
;
Protein Conformation
;
X-Ray Diffraction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
