7E1C

Structure of MreB3 from Spiroplasma eriocheiris

7E1C の概要

• エントリーDOI: 10.2210/pdb7e1c/pdb
• 分子名称: Cell shape-determining protein MreB, ACETATE ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: cytoskeleton, actin homolog, structural protein
• 由来する生物種: Spiroplasma eriocheiris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39051.60

構造登録者

Takahashi, D.,Miyata, M.,Imada, K. (登録日: 2021-02-01, 公開日: 2022-02-16, 最終更新日: 2023-11-29)

主引用文献

Takahashi, D.,Fujiwara, I.,Sasajima, Y.,Narita, A.,Imada, K.,Miyata, M.
ATP-dependent polymerization dynamics of bacterial actin proteins involved in Spiroplasma swimming.
Open Biology, 12:220083-220083, 2022

PubMed Abstract: MreB is a bacterial protein belonging to the actin superfamily. This protein polymerizes into an antiparallel double-stranded filament that determines cell shape by maintaining cell wall synthesis. , a helical wall-less bacterium, has five MreB homologous (SpeMreB1-5) that probably contribute to swimming motility. Here, we investigated the structure, ATPase activity and polymerization dynamics of SpeMreB3 and SpeMreB5. SpeMreB3 polymerized into a double-stranded filament with possible antiparallel polarity, while SpeMreB5 formed sheets which contained the antiparallel filament, upon nucleotide binding. SpeMreB3 showed slow P release owing to the lack of an amino acid motif conserved in the catalytic centre of MreB family proteins. Our SpeMreB3 crystal structures and analyses of SpeMreB3 and SpeMreB5 variants showed that the amino acid motif probably plays a role in eliminating a nucleophilic water proton during ATP hydrolysis. Sedimentation assays suggest that SpeMreB3 has a lower polymerization activity than SpeMreB5, though their polymerization dynamics are qualitatively similar to those of other actin superfamily proteins, in which pre-ATP hydrolysis and post-P release states are unfavourable for them to remain as filaments.

PubMed: 36285441
DOI: 10.1098/rsob.220083

実験手法

X-RAY DIFFRACTION (1.9 Å)