2IDC

Structure of the Histone H3-Asf1 Chaperone Interaction

Summary for 2IDC

• Entry DOI: 10.2210/pdb2idc/pdb
• Related: 1ROC
• Descriptor: ANTI-SILENCING PROTEIN 1 AND HISTONE H3 CHIMERA (2 entities in total)
• Functional Keywords: ig-like fold, asf1, h3, histone, chaperone, chromatin, replication-chaperone complex, replication/chaperone
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P61830
• Total number of polymer chains: 1
• Total formula weight: 20084.73

Authors

Antczak, A.J.,Tsubota, T.,Kaufman, P.D.,Berger, J.M. (deposition date: 2006-09-14, release date: 2007-01-30, Last modification date: 2023-08-30)

Primary citation

Antczak, A.J.,Tsubota, T.,Kaufman, P.D.,Berger, J.M.
Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics.
Bmc Struct.Biol., 6:26-26, 2006

PubMed Abstract: 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.

PubMed: 17166288
DOI: 10.1186/1472-6807-6-26

Experimental method

X-RAY DIFFRACTION (2.2 Å)