2aro

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2aro.gif|left|200px]]<br /><applet load="2aro" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2aro.gif|left|200px]]
-
caption="2aro, resolution 2.10&Aring;" />
+
 
-
'''Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione'''<br />
+
{{Structure
 +
|PDB= 2aro |SIZE=350|CAPTION= <scene name='initialview01'>2aro</scene>, resolution 2.10&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2ARO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARO OCA].
+
2ARO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARO OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16920041 16920041]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/16920041 16920041]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 26: Line 35:
[[Category: oxidation]]
[[Category: oxidation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:17 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:53:01 2008''

Revision as of 13:53, 20 March 2008

Image:2aro.gif


PDB ID 2aro

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 15:53:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2aro"
Personal tools