5MG8
Crystal structure of the S.pombe Smc5/6 hinge domain
5MG8 の概要
エントリーDOI | 10.2210/pdb5mg8/pdb |
分子名称 | Structural maintenance of chromosomes protein 5, Structural maintenance of chromosomes protein 6, SULFATE ION, ... (5 entities in total) |
機能のキーワード | smc, structural maintenance of chromosomes, hinge domain, smc5, smc6, smc5/6, recombination |
由来する生物種 | Schizosaccharomyces pombe (Fission yeast) 詳細 |
細胞内の位置 | Nucleus : O13710 P53692 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 148924.83 |
構造登録者 | |
主引用文献 | Alt, A.,Dang, H.Q.,Wells, O.S.,Polo, L.M.,Smith, M.A.,McGregor, G.A.,Welte, T.,Lehmann, A.R.,Pearl, L.H.,Murray, J.M.,Oliver, A.W. Specialized interfaces of Smc5/6 control hinge stability and DNA association. Nat Commun, 8:14011-14011, 2017 Cited by PubMed Abstract: The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is scaffolded by a specific SMC protein dimer (heterodimer in eukaryotes) held together via their hinge domains. Here we show that the Smc5/6-hinge, like those of cohesin and condensin, also forms a toroidal structure but with distinctive subunit interfaces absent from the other SMC complexes; an unusual 'molecular latch' and a functional 'hub'. Defined mutations in these interfaces cause severe phenotypic effects with sensitivity to DNA-damaging agents in fission yeast and reduced viability in human cells. We show that the Smc5/6-hinge complex binds preferentially to ssDNA and that this interaction is affected by both 'latch' and 'hub' mutations, suggesting a key role for these unique features in controlling DNA association by the Smc5/6 complex. PubMed: 28134253DOI: 10.1038/ncomms14011 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.75 Å) |
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