1WG3
Structural analysis of yeast nucleosome-assembly factor CIA1p
1WG3 の概要
| エントリーDOI | 10.2210/pdb1wg3/pdb |
| 分子名称 | Anti-silencing protein 1 (2 entities in total) |
| 機能のキーワード | beta-sandwich, riken structural genomics/proteomics initiative, rsgi, structural genomics, replication |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
| 細胞内の位置 | Nucleus: P32447 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19588.89 |
| 構造登録者 | Padmanabhan, B.,Kataoka, K.,Umehara, T.,Adachi, N.,Yokoyama, S.,Horikoshi, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-05-27, 公開日: 2005-06-14, 最終更新日: 2023-10-25) |
| 主引用文献 | 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 Cited by 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: 16428312DOI: 10.1093/jb/mvi182 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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