5YBB

Structural basis underlying complex assembly andconformational transition of the type I R-M system

5YBB の概要

• エントリーDOI: 10.2210/pdb5ybb/pdb
• 分子名称: Type I restriction-modification system methyltransferase subunit, Restriction endonuclease S subunits, DNA, ... (5 entities in total)
• 機能のキーワード: protein complex typei rm system mtase ecoki, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 338012.02

構造登録者

Liu, Y.P.,Tang, Q.,Zhang, J.Z.,Tian, L.F.,Gao, P.,Yan, X.X. (登録日: 2017-09-04, 公開日: 2017-11-29, 最終更新日: 2024-11-06)

主引用文献

Liu, Y.P.,Tang, Q.,Zhang, J.Z.,Tian, L.F.,Gao, P.,Yan, X.X.
Structural basis underlying complex assembly and conformational transition of the type I R-M system.
Proc. Natl. Acad. Sci. U.S.A., 114:11151-11156, 2017

PubMed Abstract: Type I restriction-modification (R-M) systems are multisubunit enzymes with separate DNA-recognition (S), methylation (M), and restriction (R) subunits. Despite extensive studies spanning five decades, the detailed molecular mechanisms underlying subunit assembly and conformational transition are still unclear due to the lack of high-resolution structural information. Here, we report the atomic structure of a type I MTase complex (2M+1S) bound to DNA and cofactor S-adenosyl methionine in the "open" form. The intermolecular interactions between M and S subunits are mediated by a four-helix bundle motif, which also determines the specificity of the interaction. Structural comparison between open and previously reported low-resolution "closed" structures identifies the huge conformational changes within the MTase complex. Furthermore, biochemical results show that R subunits prefer to load onto the closed form MTase. Based on our results, we proposed an updated model for the complex assembly. The work reported here provides guidelines for future applications in molecular biology.

PubMed: 28973912
DOI: 10.1073/pnas.1711754114

実験手法

X-RAY DIFFRACTION (3.2 Å)