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PDBsum entry 1hio
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Chromosomal protein
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PDB id
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1hio
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Contents |
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95 a.a.*
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90 a.a.*
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93 a.a.*
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76 a.a.*
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* C-alpha coords only
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References listed in PDB file
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Key reference
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Title
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The nucleosomal core histone octamer at 3.1 a resolution: a tripartite protein assembly and a left-Handed superhelix.
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Authors
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G.Arents,
R.W.Burlingame,
B.C.Wang,
W.E.Love,
E.N.Moudrianakis.
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Ref.
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Proc Natl Acad Sci U S A, 1991,
88,
10148-10152.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 3.
FIG. 3. Three orthogonal of the histone octamer. (a) View
showing the tripartite nature of the histone looking down
the molecular twofold axis with the superhelical axis running hori-
zontally from left to right. We refer to this as the front view. (b)
Protein wedge as it appears by looking down at a plane containing the
twofold and the superhelical axes, with the twofold axis running from
top to bottom. The apex of the wedge is formed by the
tetramer, while the H2A-H2B dimers form the lobes of the wedge. (c)
View showing the histone octamer as a disk, looking down into the
superhelical axis with the twofold axis Protrusions from
the curved surface are due to the termini of H2A, H2B, and H3.
Surfaces were calculated from a-carbon positions at twice the van
der Waals radius. The H2A-H2B dimers dark and the
tetramer is white.
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Figure 5.
FIG. 5. Stereo pair of the H2A-H2B and H3-H4 dimer domains
within the histone octamer, viewed approximately down the superhelical
axis so as to optimize visualization of the four chains and the
histone fold. For reasons of clarity, only one of each histone pair is
shown. The amino end of each chain in the model is marked by an
arrow.
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Secondary reference #1
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Title
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Spectropolarimetric analysis of the core histone octamer and its subunits.
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Authors
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J.E.Godfrey,
A.D.Baxevanis,
E.N.Moudrianakis.
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Ref.
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Biochemistry, 1990,
29,
965-972.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Crystallographic structure of the octameric histone core of the nucleosome at a resolution of 3.3 a.
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Authors
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R.W.Burlingame,
W.E.Love,
B.C.Wang,
R.Hamlin,
H.X.Nguyen,
E.N.Moudrianakis.
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Ref.
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Science, 1985,
228,
546-553.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Crystals of the octameric histone core of the nucleosome.
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Authors
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R.W.Burlingame,
W.E.Love,
E.N.Moudrianakis.
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Ref.
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Science, 1984,
223,
413-414.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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Reversible association of calf thymus histones to form the symmetrical octamer (h2ah2bh3h4)2: a case of a mixed-Associating system.
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Authors
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J.E.Godfrey,
T.H.Eickbush,
E.N.Moudrianakis.
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Ref.
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Biochemistry, 1980,
19,
1339-1346.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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The histone core complex: an octamer assembled by two sets of protein-Protein interactions.
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Authors
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T.H.Eickbush,
E.N.Moudrianakis.
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Ref.
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Biochemistry, 1978,
17,
4955-4964.
[DOI no: ]
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PubMed id
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Secondary reference #6
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Title
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The compaction of DNA helices into either continuous supercoils or folded-Fiber rods and toroids.
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Authors
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T.H.Eickbush,
E.N.Moudrianakis.
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Ref.
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Cell, 1978,
13,
295-306.
[DOI no: ]
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PubMed id
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Headers
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