1WG3

Structural analysis of yeast nucleosome-assembly factor CIA1p

Summary for 1WG3

• Entry DOI: 10.2210/pdb1wg3/pdb
• Descriptor: Anti-silencing protein 1 (2 entities in total)
• Functional Keywords: beta-sandwich, riken structural genomics/proteomics initiative, rsgi, structural genomics, replication
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P32447
• Total number of polymer chains: 1
• Total formula weight: 19588.89

Authors

Padmanabhan, B.,Kataoka, K.,Umehara, T.,Adachi, N.,Yokoyama, S.,Horikoshi, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-27, release date: 2005-06-14, Last modification date: 2023-10-25)

Primary citation

Padmanabhan, B.,Kataoka, K.,Umehara, T.,Adachi, N.,Yokoyama, S.,Horikoshi, M.
Structural Similarity between Histone Chaperone Cia1p/Asf1p and DNA-Binding Protein NF-{kappa}B
J.Biochem.(Tokyo), 138:821-829, 2005

PubMed Abstract: The structural relationships between histone-binding proteins and DNA-binding proteins are important, since nucleosome-interacting factors possess histone-binding and/or DNA-binding components. S. cerevisiae (Sc) Cia1p/Asf1p, a homologue of human CIA (CCG1-interacting factor A), is the most evolutionarily conserved histone chaperone, which facilitates nucleosome assembly by interacting with the nucleosome entry site of the core histones H3/H4. The crystal structure of the evolutionarily conserved domain (residues 1-169) of Cia1p (ScCia1p-DeltaC2) was determined at 2.95 A resolution. The refined model contains 166 residues in the asymmetric unit. The overall tertiary structure resembles a beta-sandwich fold, and belongs to the "switched" immunoglobulin class of proteins. The crystal structure suggests that ScCia1p-DeltaC2 is structurally related to the DNA-binding proteins, such as NF-kappaB and its family members. This is the first examination of the structural similarities between a histone chaperone and DNA-binding proteins. We discuss the possibilities that the strands beta3 and beta4, which possess highly electronegative surface potentials, are the important regions for the interaction with core histones, and that the histone chaperone ScCia1p/Asf1p and the DNA-binding protein NF-kappaB may have evolved from the same prototypal protein class.

PubMed: 16428312
DOI: 10.1093/jb/mvi182

Experimental method

X-RAY DIFFRACTION (3 Å)