2WD5

SMC hinge heterodimer (Mouse)

2WD5 の概要

• エントリーDOI: 10.2210/pdb2wd5/pdb
• 分子名称: STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 1A, STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3 (3 entities in total)
• 機能のキーワード: dna damage, cell cycle, cell division
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Nucleus: Q9CU62 Q9CW03
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51167.70

構造登録者

Michie, K.A.,Haering, C.H.,Nasmyth, K.,Lowe, J. (登録日: 2009-03-20, 公開日: 2010-08-11, 最終更新日: 2024-05-08)

主引用文献

Kurze, A.,Michie, K.A.,Dixon, S.E.,Mishra, A.,Itoh, T.,Khalid, S.,Strmecki, L.,Shirahige, K.,Haering, C.H.,Lowe, J.,Nasmyth, K.
A Positively Charged Channel within the Smc1/Smc3 Hinge Required for Sister Chromatid Cohesion.
Embo J., 30:364-, 2011

PubMed Abstract: Cohesin's structural maintenance of chromosome 1 (Smc1) and Smc3 are rod-shaped proteins with 50-nm long intra-molecular coiled-coil arms with a heterodimerization domain at one end and an ABC-like nucleotide-binding domain (NBD) at the other. Heterodimerization creates V-shaped molecules with a hinge at their centre. Inter-connection of NBDs by Scc1 creates a tripartite ring within which, it is proposed, sister DNAs are entrapped. To investigate whether cohesin's hinge functions as a possible DNA entry gate, we solved the crystal structure of the hinge from Mus musculus, which like its bacterial counterpart is characterized by a pseudo symmetric heterodimeric torus containing a small channel that is positively charged. Mutations in yeast Smc1 and Smc3 that together neutralize the channel's charge have little effect on dimerization or association with chromosomes, but are nevertheless lethal. Our finding that neutralization reduces acetylation of Smc3, which normally occurs during replication and is essential for cohesion, suggests that the positively charged channel is involved in a major conformational change during S phase.

PubMed: 21139566
DOI: 10.1038/EMBOJ.2010.315

実験手法

X-RAY DIFFRACTION (2.7 Å)