4AM6

C-TERMINAL DOMAIN OF ACTIN-RELATED PROTEIN ARP8 FROM S. CEREVISIAE

Summary for 4AM6

• Entry DOI: 10.2210/pdb4am6/pdb
• Related: 4AM7
• EMDB information: 2224 2225
• Descriptor: ACTIN-LIKE PROTEIN ARP8, SULFATE ION (3 entities in total)
• Functional Keywords: nuclear protein, chromatin remodelling complex, atp-binding protein, nuclear actin-related protein, transcription regulation, dna repair
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 149819.06

Authors

Wuerges, J.,Saravanan, M.,Bose, D.,Cook, N.J.,Zhang, X.,Wigley, D.B. (deposition date: 2012-03-07, release date: 2012-12-12, Last modification date: 2024-05-08)

Primary citation

Saravanan, M.,Wuerges, J.,Bose, D.,Mccormack, E.A.,Cook, N.J.,Zhang, X.,Wigley, D.B.
Interactions between the Nucleosome Histone Core and Arp8 in the Ino80 Chromatin Remodeling Complex.
Proc.Natl.Acad.Sci.USA, 109:20883-, 2012

PubMed Abstract: Actin-related protein Arp8 is a component of the INO80 chromatin remodeling complex. Yeast Arp8 (yArp8) comprises two domains: a 25-KDa N-terminal domain, found only in yeast, and a 75-KDa C-terminal domain (yArp8CTD) that contains the actin fold and is conserved across other species. The crystal structure shows that yArp8CTD contains three insertions within the actin core. Using a combination of biochemistry and EM, we show that Arp8 forms a complex with nucleosomes, and that the principal interactions are via the H3 and H4 histones, mediated through one of the yArp8 insertions. We show that recombinant yArp8 exists in monomeric and dimeric states, but the dimer is the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core. Taken together, these data provide unique insight into the stoichiometry, architecture, and molecular interactions between components of the INO80 remodeling complex and nucleosomes, providing a first step toward building up the structure of the complex.

PubMed: 23213201
DOI: 10.1073/PNAS.1214735109

Experimental method

X-RAY DIFFRACTION (2.7 Å)