6IZR

Whole structure of a 15-stranded ParM filament from Clostridium botulinum

6IZR の概要

• エントリーDOI: 10.2210/pdb6izr/pdb
• EMDBエントリー: 9757
• 分子名称: Putative plasmid segregation protein ParM, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: parm, filaments, cytoskeleton, protein fibril
• 由来する生物種: Clostridium botulinum Prevot_594
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1200350.22

構造登録者

Koh, F.,Narita, A.,Lee, L.J.,Tan, Y.Z.,Dandey, V.P.,Tanaka, K.,Popp, D.,Robinson, R.C. (登録日: 2018-12-20, 公開日: 2019-06-19, 最終更新日: 2024-05-29)

主引用文献

Koh, F.,Narita, A.,Lee, L.J.,Tanaka, K.,Tan, Y.Z.,Dandey, V.P.,Popp, D.,Robinson, R.C.
The structure of a 15-stranded actin-like filament from Clostridium botulinum.
Nat Commun, 10:2856-2856, 2019

PubMed Abstract: Microfilaments (actin) and microtubules represent the extremes in eukaryotic cytoskeleton cross-sectional dimensions, raising the question of whether filament architectures are limited by protein fold. Here, we report the cryoelectron microscopy structure of a complex filament formed from 15 protofilaments of an actin-like protein. This actin-like ParM is encoded on the large pCBH Clostridium botulinum plasmid. In cross-section, the ~26 nm diameter filament comprises a central helical protofilament surrounded by intermediate and outer layers of six and eight twisted protofilaments, respectively. Alternating polarity of the layers allows for similar lateral contacts between each layer. This filament design is stiffer than the actin filament, and has likely been selected for during evolution to move large cargos. The comparable sizes of microtubule and pCBH ParM filaments indicate that larger filament architectures are not limited by the protomer fold. Instead, function appears to have been the evolutionary driving force to produce broad, complex filaments.

PubMed: 31253774
DOI: 10.1038/s41467-019-10779-9

実験手法

ELECTRON MICROSCOPY (4.7 Å)