4RSJ
Pyrococcus furiosus Smc hinge domain with an extended coiled coil
4RSJ の概要
エントリーDOI | 10.2210/pdb4rsj/pdb |
関連するPDBエントリー | 4RSI |
分子名称 | Chromosome partition protein Smc (1 entity in total) |
機能のキーワード | smc hinge domain with coiled coils, cell cycle |
由来する生物種 | Pyrococcus furiosus |
細胞内の位置 | Cytoplasm : Q8TZY2 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 123441.42 |
構造登録者 | |
主引用文献 | Soh, Y.M.,Burmann, F.,Shin, H.C.,Oda, T.,Jin, K.S.,Toseland, C.P.,Kim, C.,Lee, H.,Kim, S.J.,Kong, M.S.,Durand-Diebold, M.L.,Kim, Y.G.,Kim, H.M.,Lee, N.K.,Sato, M.,Oh, B.H.,Gruber, S. Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding. Mol.Cell, 57:290-303, 2015 Cited by PubMed Abstract: SMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive "hinge" dimerization domain with an ATP-regulated "head" dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB's association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc's dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome. PubMed: 25557547DOI: 10.1016/j.molcel.2014.11.023 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.5 Å) |
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