7NYX

Cryo-EM structure of the MukBEF-MatP-DNA monomer (closed conformation)

7NYX の概要

• エントリーDOI: 10.2210/pdb7nyx/pdb
• EMDBエントリー: 12657
• 分子名称: Chromosome partition protein MukB, ADENOSINE-5'-TRIPHOSPHATE, 4'-PHOSPHOPANTETHEINE, ... (11 entities in total)
• 機能のキーワード: smc-kleisin complex, atpase, dna binding protein
• 由来する生物種: Photorhabdus thracensis; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 618624.14

構造登録者

Buermann, F.,Lowe, J. (登録日: 2021-03-23, 公開日: 2021-07-07, 最終更新日: 2022-03-23)

主引用文献

Burmann, F.,Funke, L.F.H.,Chin, J.W.,Lowe, J.
Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites.
Mol.Cell, 81:4891-4906.e8, 2021

PubMed Abstract: The ring-like structural maintenance of chromosomes (SMC) complex MukBEF folds the genome of Escherichia coli and related bacteria into large loops, presumably by active DNA loop extrusion. MukBEF activity within the replication terminus macrodomain is suppressed by the sequence-specific unloader MatP. Here, we present the complete atomic structure of MukBEF in complex with MatP and DNA as determined by electron cryomicroscopy (cryo-EM). The complex binds two distinct DNA double helices corresponding to the arms of a plectonemic loop. MatP-bound DNA threads through the MukBEF ring, while the second DNA is clamped by the kleisin MukF, MukE, and the MukB ATPase heads. Combinatorial cysteine cross-linking confirms this topology of DNA loop entrapment in vivo. Our findings illuminate how a class of near-ubiquitous DNA organizers with important roles in genome maintenance interacts with the bacterial chromosome.

PubMed: 34739874
DOI: 10.1016/j.molcel.2021.10.011

実験手法

ELECTRON MICROSCOPY (4.6 Å)