1MWM

ParM from plasmid R1 ADP form

1MWM の概要

• エントリーDOI: 10.2210/pdb1mwm/pdb
• 関連するPDBエントリー: 1MWK
• 分子名称: ParM, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: parm, structural protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72511.76

構造登録者

Van den Ent, F.,Moller-Jensen, J.,Amos, L.A.,Gerdes, K.,Lowe, J. (登録日: 2002-09-30, 公開日: 2003-01-28, 最終更新日: 2024-04-03)

主引用文献

Van den Ent, F.,Moller-Jensen, J.,Amos, L.A.,Gerdes, K.,Lowe, J.
F-actin-like filaments formed by plasmid segregation protein ParM
EMBO J., 21:6935-6943, 2002

PubMed Abstract: It was the general belief that DNA partitioning in prokaryotes is independent of a cytoskeletal structure, which in eukaryotic cells is indispensable for DNA segregation. Recently, however, immunofluorescence microscopy revealed highly dynamic, filamentous structures along the longitudinal axis of Escherichia coli formed by ParM, a plasmid-encoded protein required for accurate segregation of low-copy-number plasmid R1. We show here that ParM polymerizes into double helical protofilaments with a longitudinal repeat similar to filamentous actin (F-actin) and MreB filaments that maintain the cell shape of non-spherical bacteria. The crystal structure of ParM with and without ADP demonstrates that it is a member of the actin family of proteins and shows a domain movement of 25 degrees upon nucleotide binding. Furthermore, the crystal structure of ParM reveals major differences in the protofilament interface compared with F-actin, despite the similar arrangement of the subunits within the filaments. Thus, there is now evidence for cytoskeletal structures, formed by actin-like filaments that are involved in plasmid partitioning in E.coli.

PubMed: 12486014
DOI: 10.1093/emboj/cdf672

実験手法

X-RAY DIFFRACTION (2 Å)