2hue: Difference between revisions

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New page: left|200px<br /><applet load="2hue" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hue, resolution 1.7Å" /> '''Structure of the H3-H...
 
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[[Image:2hue.gif|left|200px]]<br /><applet load="2hue" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2hue.gif|left|200px]]<br /><applet load="2hue" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2hue, resolution 1.7&Aring;" />
caption="2hue, resolution 1.7&Aring;" />
'''Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4'''<br />
'''Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4'''<br />


==Overview==
==Overview==
Anti-silencing function 1 (Asf1) is a highly conserved chaperone of, histones H3/H4 that assembles or disassembles chromatin during, transcription, replication, and repair. The structure of the globular, domain of Asf1 bound to H3/H4 determined by X-ray crystallography to a, resolution of 1.7 Angstroms shows how Asf1 binds the H3/H4 heterodimer, enveloping the C terminus of histone H3 and physically blocking formation, of the H3/H4 heterotetramer. Unexpectedly, the C terminus of histone H4, that forms a mini-beta sheet with histone H2A in the nucleosome undergoes, a major conformational change upon binding to Asf1 and adds a beta strand, to the Asf1 beta sheet sandwich. Interactions with both H3 and H4 were, required for Asf1 histone chaperone function in vivo and in vitro. The, Asf1-H3/H4 structure suggests a "strand-capture" mechanism whereby the H4, tail acts as a lever to facilitate chromatin disassembly/assembly that may, be used ubiquitously by histone chaperones.
Anti-silencing function 1 (Asf1) is a highly conserved chaperone of histones H3/H4 that assembles or disassembles chromatin during transcription, replication, and repair. The structure of the globular domain of Asf1 bound to H3/H4 determined by X-ray crystallography to a resolution of 1.7 Angstroms shows how Asf1 binds the H3/H4 heterodimer, enveloping the C terminus of histone H3 and physically blocking formation of the H3/H4 heterotetramer. Unexpectedly, the C terminus of histone H4 that forms a mini-beta sheet with histone H2A in the nucleosome undergoes a major conformational change upon binding to Asf1 and adds a beta strand to the Asf1 beta sheet sandwich. Interactions with both H3 and H4 were required for Asf1 histone chaperone function in vivo and in vitro. The Asf1-H3/H4 structure suggests a "strand-capture" mechanism whereby the H4 tail acts as a lever to facilitate chromatin disassembly/assembly that may be used ubiquitously by histone chaperones.


==About this Structure==
==About this Structure==
2HUE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with SO4, ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HUE OCA].  
2HUE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HUE OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Churchill, M.E.A.]]
[[Category: Churchill, M E.A.]]
[[Category: English, C.M]]
[[Category: English, C M]]
[[Category: Tyler, J.K.]]
[[Category: Tyler, J K.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: mini beta sheet]]
[[Category: mini beta sheet]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:48 2008''