4APW

Alp12 filament structure

4APW の概要

• エントリーDOI: 10.2210/pdb4apw/pdb
• EMDBエントリー: 2068
• 分子名称: ALP12 (1 entity in total)
• 機能のキーワード: structural protein, alp12, actin-like protein
• 由来する生物種: CLOSTRIDIUM TETANI
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 591871.25

構造登録者

Popp, D.,Narita, A.,Lee, L.J.,Ghoshdastider, U.,Xue, B.,Srinivasan, R.,Balasubramanian, M.K.,Tanaka, T.,Robinson, R.C. (登録日: 2012-04-06, 公開日: 2012-05-16, 最終更新日: 2024-05-08)

主引用文献

Popp, D.,Narita, A.,Lee, L.J.,Ghoshdastider, U.,Xue, B.,Srinivasan, R.,Balasubramanian, M.K.,Tanaka, T.,Robinson, R.C.
Novel Actin-Like Filament Structure from Clostridium Tetani.
J.Biol.Chem., 287:21121-, 2012

PubMed Abstract: Eukaryotic F-actin is constructed from two protofilaments that gently wind around each other to form a helical polymer. Several bacterial actin-like proteins (Alps) are also known to form F-actin-like helical arrangements from two protofilaments, yet with varied helical geometries. Here, we report a unique filament architecture of Alp12 from Clostridium tetani that is constructed from four protofilaments. Through fitting of an Alp12 monomer homology model into the electron microscopy data, the filament was determined to be constructed from two antiparallel strands, each composed of two parallel protofilaments. These four protofilaments form an open helical cylinder separated by a wide cleft. The molecular interactions within single protofilaments are similar to F-actin, yet interactions between protofilaments differ from those in F-actin. The filament structure and assembly and disassembly kinetics suggest Alp12 to be a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin, and thus a potential target for drug design. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.

PubMed: 22514279
DOI: 10.1074/JBC.M112.341016

実験手法

ELECTRON MICROSCOPY (19.7 Å)