5AEY

actin-like ParM protein bound to AMPPNP

5AEY の概要

• エントリーDOI: 10.2210/pdb5aey/pdb
• EMDBエントリー: 2850
• 分子名称: PLASMID SEGREGATION PROTEIN PARM, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total)
• 機能のキーワード: structural protein, bacterial cytoskeleton, plasmid segregation, actin- like protein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 180697.10

構造登録者

Bharat, T.A.M.,Murshudov, G.N.,Sachse, C.,Lowe, J. (登録日: 2015-01-12, 公開日: 2015-04-22, 最終更新日: 2024-05-08)

主引用文献

Bharat, T.A.M.,Murshudov, G.N.,Sachse, C.,Lowe, J.
Structures of Actin-Like Parm Filaments Show Architecture of Plasmid-Segregating Spindles.
Nature, 523:106-, 2015

PubMed Abstract: Active segregation of Escherichia coli low-copy-number plasmid R1 involves formation of a bipolar spindle made of left-handed double-helical actin-like ParM filaments. ParR links the filaments with centromeric parC plasmid DNA, while facilitating the addition of subunits to ParM filaments. Growing ParMRC spindles push sister plasmids to the cell poles. Here, using modern electron cryomicroscopy methods, we investigate the structures and arrangements of ParM filaments in vitro and in cells, revealing at near-atomic resolution how subunits and filaments come together to produce the simplest known mitotic machinery. To understand the mechanism of dynamic instability, we determine structures of ParM filaments in different nucleotide states. The structure of filaments bound to the ATP analogue AMPPNP is determined at 4.3 Å resolution and refined. The ParM filament structure shows strong longitudinal interfaces and weaker lateral interactions. Also using electron cryomicroscopy, we reconstruct ParM doublets forming antiparallel spindles. Finally, with whole-cell electron cryotomography, we show that doublets are abundant in bacterial cells containing low-copy-number plasmids with the ParMRC locus, leading to an asynchronous model of R1 plasmid segregation.

PubMed: 25915019
DOI: 10.1038/NATURE14356

実験手法

ELECTRON MICROSCOPY (4.3 Å)