1hio: Difference between revisions

Revision as of 08:14, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hio.png

Template:STRUCTURE 1hio

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

Template:ABSTRACT PUBMED 1946434

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

Page seeded by OCA on Tue Jul 1 08:14:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1hio.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1hio|  PDB=1hio  |  SCENE=  }}
-'''HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY'''
+===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. &amp; 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_1946434}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1946434 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1946434}}
 ==About this Structure==
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 [[Category: Histone]]
 [[Category: Nucleosome core]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:53:02 2008''
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