4UX3
cohesin Smc3-HD:Scc1-N complex from yeast
4UX3 の概要
エントリーDOI | 10.2210/pdb4ux3/pdb |
分子名称 | STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3, MITOTIC CHROMOSOME DETERMINANT-RELATED PROTEIN, MAGNESIUM ION, ... (4 entities in total) |
機能のキーワード | protein binding, cohesin, mitosis, chromosome segregation, kleisin, smc |
由来する生物種 | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) 詳細 |
細胞内の位置 | Nucleus: P47037 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 76108.76 |
構造登録者 | |
主引用文献 | Gligoris, T.G.,Scheinost, J.C.,Burmann, F.,Petela, N.,Chan, K.,Uluocak, P.,Beckouet, F.,Gruber, S.,Nasmyth, K.,Lowe, J. Closing the Cohesin Ring: Structure and Function of its Smc3-Kleisin Interface. Science, 346:963-, 2014 Cited by PubMed Abstract: Through their association with a kleisin subunit (Scc1), cohesin's Smc1 and Smc3 subunits are thought to form tripartite rings that mediate sister chromatid cohesion. Unlike the structure of Smc1/Smc3 and Smc1/Scc1 interfaces, that of Smc3/Scc1 is not known. Disconnection of this interface is thought to release cohesin from chromosomes in a process regulated by acetylation. We show here that the N-terminal domain of yeast Scc1 contains two α helices, forming a four-helix bundle with the coiled coil emerging from Smc3's adenosine triphosphatase head. Mutations affecting this interaction compromise cohesin's association with chromosomes. The interface is far from Smc3 residues, whose acetylation prevents cohesin's dissociation from chromosomes. Cohesin complexes holding chromatids together in vivo do indeed have the configuration of hetero-trimeric rings, and sister DNAs are entrapped within these. PubMed: 25414305DOI: 10.1126/SCIENCE.1256917 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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