2idc: Difference between revisions
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'''Structure of the Histone H3-Asf1 Chaperone Interaction''' | {{Structure | ||
|PDB= 2idc |SIZE=350|CAPTION= <scene name='initialview01'>2idc</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= ASF1 and HHT1, SIN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Structure of the Histone H3-Asf1 Chaperone Interaction''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2IDC is a [ | 2IDC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IDC OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics., Antczak AJ, Tsubota T, Kaufman PD, Berger JM, BMC Struct Biol. 2006 Dec 13;6:26. PMID:[http:// | Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics., Antczak AJ, Tsubota T, Kaufman PD, Berger JM, BMC Struct Biol. 2006 Dec 13;6:26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17166288 17166288] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ig-like fold]] | [[Category: ig-like fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:28:09 2008'' | ||
Revision as of 15:28, 20 March 2008
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| 2idc, resolution 2.20Å | |||||||||||||
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| Gene: | ASF1 and HHT1, SIN2 (Saccharomyces cerevisiae) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of the Histone H3-Asf1 Chaperone Interaction
Overview
BACKGROUND: The histone H3/H4 chaperone Asf1 (anti-silencing function 1) is required for the establishment and maintenance of proper chromatin structure, as well as for genome stability in eukaryotes. Asf1 participates in both DNA replication-coupled (RC) and replication-independent (RI) histone deposition reactions in vitro and interacts with complexes responsible for both pathways in vivo. Asf1 is known to directly bind histone H3, however, high-resolution structural information about the geometry of this interaction was previously unknown. RESULTS: Here we report the structure of a histone/histone chaperone interaction. We have solved the 2.2 A crystal structure of the conserved N-terminal immunoglobulin fold domain of yeast Asf1 (residues 2-155) bound to the C-terminal helix of yeast histone H3 (residues 121-134). The structure defines a histone-binding patch on Asf1 consisting of both conserved and yeast-specific residues; mutation of these residues abrogates H3/H4 binding affinity. The geometry of the interaction indicates that Asf1 binds to histones H3/H4 in a manner that likely blocks sterically the H3/H3 interface of the nucleosomal four-helix bundle. CONCLUSION: These data clarify how Asf1 regulates histone stoichiometry to modulate epigenetic inheritance. The structure further suggests a physical model in which Asf1 contributes to interpretation of a "histone H3 barcode" for sorting H3 isoforms into different deposition pathways.
About this Structure
2IDC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics., Antczak AJ, Tsubota T, Kaufman PD, Berger JM, BMC Struct Biol. 2006 Dec 13;6:26. PMID:17166288
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