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| - | [[Image:2aro.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2aro| PDB=2aro | SCENE= }} | | {{STRUCTURE_2aro| PDB=2aro | SCENE= }} |
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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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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16920041}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16920041 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16920041}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Octamer]] | | [[Category: Octamer]] |
| | [[Category: Oxidation]] | | [[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 Tue Jul 29 15:02:09 2008'' |
Revision as of 12:02, 29 July 2008
Template:STRUCTURE 2aro
Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
Template:ABSTRACT PUBMED 16920041
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 Tue Jul 29 15:02:09 2008
