7RTX

Actophorin grown in microgravity

7RTX の概要

• エントリーDOI: 10.2210/pdb7rtx/pdb
• 分子名称: Actophorin (2 entities in total)
• 機能のキーワード: microgravity, motor protein
• 由来する生物種: Acanthamoeba castellanii (Amoeba)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15444.39

構造登録者

Lieberman, R.L.,Quirk, S. (登録日: 2021-08-16, 公開日: 2021-12-22, 最終更新日: 2023-10-18)

主引用文献

Quirk, S.,Lieberman, R.L.
Improved resolution crystal structure of Acanthamoeba actophorin reveals structural plasticity not induced by microgravity.
Acta Crystallogr.,Sect.F, 77:452-458, 2021

PubMed Abstract: Actophorin, a protein that severs actin filaments isolated from the amoeba Acanthamoeba castellanii, was employed as a test case for crystallization under microgravity. Crystals of purified actophorin were grown under microgravity conditions aboard the International Space Station (ISS) utilizing an interactive crystallization setup between the ISS crew and ground-based experimenters. Crystals grew in conditions similar to those grown on earth. The structure was solved by molecular replacement at a resolution of 1.65 Å. Surprisingly, the structure reveals conformational changes in a remote β-turn region that were previously associated with actophorin phosphorylated at the terminal residue Ser1. Although crystallization under microgravity did not yield a higher resolution than crystals grown under typical laboratory conditions, the conformation of actophorin obtained from solving the structure suggests greater flexibility in the actophorin β-turn than previously appreciated and may be beneficial for the binding of actophorin to actin filaments.

PubMed: 34866600
DOI: 10.1107/S2053230X21011419

実験手法

X-RAY DIFFRACTION (1.65 Å)