3HTK

Crystal structure of Mms21 and Smc5 complex

3HTK の概要

• エントリーDOI: 10.2210/pdb3htk/pdb
• 分子名称: Structural maintenance of chromosomes protein 5, E3 SUMO-protein ligase MMS21, ZINC ION, ... (5 entities in total)
• 機能のキーワード: sumo e3 ligase, spl-ring, ring, atp-binding, chromosomal protein, coiled coil, dna damage, dna recombination, dna repair, nucleotide-binding, nucleus, ubl conjugation, cytoplasm, ligase, metal-binding, ubl conjugation pathway, zinc, zinc-finger, recombination-replication-ligase complex, recombination/replication/ligase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); 詳細
• 細胞内の位置: Nucleus (Potential): Q08204 Q08204; Nucleus: P38632
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46198.82

構造登録者

Duan, X.,Sarangi, P.,Liu, X.,Rangi, G.K.,Zhao, X.,Ye, H. (登録日: 2009-06-11, 公開日: 2009-10-20, 最終更新日: 2024-02-21)

主引用文献

Duan, X.,Sarangi, P.,Liu, X.,Rangi, G.K.,Zhao, X.,Ye, H.
Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex.
Mol.Cell, 35:657-668, 2009

PubMed Abstract: The Smc5/6 complex is an evolutionarily conserved chromosomal ATPase required for cell growth and DNA repair. Its Mms21 subunit supports both functions by docking to the arm region of Smc5 and providing SUMO ligase activity. Here, we report the crystal structure of Mms21 in complex with the Smc5 arm. Our structure revealed two distinct structural and functional domains of the Smc5-bound Mms21: its N-terminal half is dedicated to Smc5 binding by forming a helix bundle with a coiled-coil structure of Smc5; its C-terminal half includes the SUMO ligase domain, which adopts a new type of RING E3 structure. Mutagenesis and structural analyses showed that the Mms21-Smc5 interface is required for cell growth and resistance to DNA damage, while the unique Mms21 RING domain confers specificity to the SUMO E2-E3 interaction. Through structure-based dissection of Mms21 functions, our studies establish a framework for understanding its roles in the Smc5/6 complex.

PubMed: 19748359
DOI: 10.1016/j.molcel.2009.06.032

実験手法

X-RAY DIFFRACTION (2.31 Å)