2YFV
The heterotrimeric complex of Kluyveromyces lactis Scm3, Cse4 and H4
2YFV の概要
| エントリーDOI | 10.2210/pdb2yfv/pdb |
| 関連するPDBエントリー | 2YFW |
| 分子名称 | HISTONE H3-LIKE CENTROMERIC PROTEIN CSE4, HISTONE H4, SCM3, ... (5 entities in total) |
| 機能のキーワード | cell cycle, kinetochore, centromere, histone chaperone, budding yeast |
| 由来する生物種 | KLUYVEROMYCES LACTIS NRRL Y-1140 詳細 |
| 細胞内の位置 | Nucleus (By similarity): Q6CTI2 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 27833.85 |
| 構造登録者 | |
| 主引用文献 | Cho, U.S.,Harrison, S.C. Recognition of the Centromere-Specific Histone Cse4 by the Chaperone Scm3. Proc.Natl.Acad.Sci.USA, 108:9367-, 2011 Cited by PubMed Abstract: A specialized nucleosome is a component of all eukaryotic kinetochores. The core of this nucleosome contains a centromere-specific histone, CENP-A (the Cse4 gene product in budding yeast), instead of the usual H3. Assembly of a centromeric nucleosome depends on a specific chaperone, called Scm3 in yeast and HJURP in higher eukaryotes. We describe here the structure of a complex formed by an N-terminal fragment of Scm3 with the histone-fold domains of Cse4, and H4, all prepared as recombinant proteins derived from the budding yeast Kluyveromyces lactis. The contacts of Scm3 with Cse4 explain its selectivity for the centromere-specific histone; key residues at the interface are conserved in HJURP, indicating a common mechanism for centromeric-histone deposition. We also report the structure of a (Cse4 : H4)(2) heterotetramer; comparison with the structure of the Scm3:Cse4:H4 complex shows that tetramer formation and DNA-binding require displacement of Scm3 from the nucleosome core. The two structures together suggest that specific contacts between the chaperone and Cse4, rather than an altered overall structure of the nucleosome core, determine the selective presence of Cse4 at centromeres. PubMed: 21606327DOI: 10.1073/PNAS.1106389108 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.32 Å) |
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