2aro
From Proteopedia
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[[Image:2aro.gif|left|200px]] | [[Image:2aro.gif|left|200px]] | ||
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'''Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione''' | '''Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione''' | ||
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[[Category: Sodngam, S.]] | [[Category: Sodngam, S.]] | ||
[[Category: Wood, C M.]] | [[Category: Wood, C M.]] | ||
| - | [[Category: | + | [[Category: Allostery]] |
| - | [[Category: | + | [[Category: Circular dichroism]] |
| - | [[Category: | + | [[Category: Octamer]] |
| - | [[Category: | + | [[Category: Oxidation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:23:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:23, 3 May 2008
Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
Overview
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.
About this Structure
2ARO is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
Reference
The oxidised histone octamer does not form a H3 disulphide bond., Wood CM, Sodngam S, Nicholson JM, Lambert SJ, Reynolds CD, Baldwin JP, Biochim Biophys Acta. 2006 Aug;1764(8):1356-62. Epub 2006 Jul 21. PMID:16920041 Page seeded by OCA on Sat May 3 19:23:34 2008
