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PDBsum entry 2aro
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Structural protein
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PDB id
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2aro
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Contents |
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106 a.a.
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92 a.a.
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95 a.a.
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83 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Structural protein
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Title:
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Crystal structure of the native histone octamer to 2.1 angstrom resolution, crystalised in the presence of s-nitrosoglutathione
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Structure:
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Histone h2a-iv. Chain: a, e. Histone h2b. Chain: b, f. Histone h3. Chain: c, g. Histone h4-vi. Chain: d, h
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Organism_taxid: 9031
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Biol. unit:
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Octamer (from
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Resolution:
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2.10Å
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R-factor:
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0.186
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R-free:
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0.225
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Authors:
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C.M.Wood,S.Sodngam,J.M.Nicholson,S.J.Lambert,C.D.Reynolds,J.P.Baldwin
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Key ref:
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C.M.Wood
et al.
(2006).
The oxidised histone octamer does not form a H3 disulphide bond.
Biochim Biophys Acta,
1764,
1356-1362.
PubMed id:
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Date:
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20-Aug-05
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Release date:
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30-Aug-05
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PROCHECK
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Headers
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References
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P02263
(H2A4_CHICK) -
Histone H2A-IV from Gallus gallus
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Seq:
Struc:
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129 a.a.
106 a.a.
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P0C1H3
(H2B1_CHICK) -
Histone H2B 1/2/3/4/6 from Gallus gallus
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Seq:
Struc:
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126 a.a.
92 a.a.
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Biochim Biophys Acta
1764:1356-1362
(2006)
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PubMed id:
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The oxidised histone octamer does not form a H3 disulphide bond.
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C.M.Wood,
S.Sodngam,
J.M.Nicholson,
S.J.Lambert,
C.D.Reynolds,
J.P.Baldwin.
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ABSTRACT
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A H3 dimer band is produced when purified native histone octamers are run on an
SDS-PAGE gel in a beta-mercaptoethanol-free environment. To investigate this,
native histone octamer crystals, derived from chicken erythrocytes, and of
structure (H2A-H2B)-(H4-H3)-(H3'-H4')-(H2B'-H2A'), were grown in 2 M KCl, 1.35 M
potassium phosphates and 250-350 microM of the oxidising agent
S-nitrosoglutathione, pH 6.9. X-ray diffraction data were acquired to 2.10 A
resolution, yielding a structure with an Rwork value of 18.6% and an Rfree of
22.5%. The space group is P6(5), the asymmetric unit of which contains one
complete octamer. Compared to the 1.90 A resolution, unoxidised native histone
octamer structure, the crystals show a reduction of 2.5% in the c-axis of the
unit cell, and free-energy calculations reveal that the H3-H3' dimer interface
in the latter has become thermodynamically stable, in contrast to the former.
Although the inter-sulphur distance of the two H3 cysteines in the oxidised
native histone octamer has reduced to 6 A from the 7 A of the unoxidised form,
analysis of the hydrogen bonds that constitute the (H4-H3)-(H3'-H4') tetramer
indicates that the formation of a disulphide bond in the H3-H3' dimer interface
is incompatible with stable tetramer formation. The biochemical and biophysical
evidence, taken as a whole, is indicative of crystals that have a stable H3-H3'
dimer interface, possibly extending to the interface within an isolated H3-H3'
dimer, observed in SDS-PAGE gels.
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