6BQW

AlfA Filament bound to AMPPNP

6BQW の概要

• エントリーDOI: 10.2210/pdb6bqw/pdb
• EMDBエントリー: 7134
• 分子名称: Bacterial actin AlfA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total)
• 機能のキーワード: actin, plasmid segregation, filament, cytosolic protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 284909.49

構造登録者

Usluer, G.D.,Kollman, J.M.,DiMaio, F. (登録日: 2017-11-28, 公開日: 2018-02-28, 最終更新日: 2024-03-13)

主引用文献

Usluer, G.D.,DiMaio, F.,Yang, S.K.,Hansen, J.M.,Polka, J.K.,Mullins, R.D.,Kollman, J.M.
Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.
Proc. Natl. Acad. Sci. U.S.A., 115:3356-3361, 2018

PubMed Abstract: Bacterial actins are an evolutionarily diverse family of ATP-dependent filaments built from protomers with a conserved structural fold. Actin-based segregation systems are encoded on many bacterial plasmids and function to partition plasmids into daughter cells. The bacterial actin AlfA segregates plasmids by a mechanism distinct from other partition systems, dependent on its unique dynamic properties. Here, we report the near-atomic resolution electron cryo-microscopy structure of the AlfA filament, which reveals a strikingly divergent filament architecture resulting from the loss of a subdomain conserved in all other actins and a mode of ATP binding. Its unusual assembly interfaces and nucleotide interactions provide insight into AlfA dynamics, and expand the range of evolutionary variation accessible to actin quaternary structure.

PubMed: 29440491
DOI: 10.1073/pnas.1715836115

実験手法

ELECTRON MICROSCOPY (4.2 Å)