6I7D
Plasmodium falciparum Myosin A, post-rigor and rigor-like states
6I7D の概要
エントリーDOI | 10.2210/pdb6i7d/pdb |
分子名称 | Myosin-A, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total) |
機能のキーワード | myosin a, plasmodium falciparum, tunable mechanism, motor protein |
由来する生物種 | Plasmodium falciparum (isolate 3D7) |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 346492.98 |
構造登録者 | Robert-Paganin, J.,Auguin, D.,Moussaoui, D.,Jousset, G.,Baum, J.,Trybus, K.M.,Houdusse, A. (登録日: 2018-11-16, 公開日: 2019-08-07, 最終更新日: 2024-01-24) |
主引用文献 | Robert-Paganin, J.,Robblee, J.P.,Auguin, D.,Blake, T.C.A.,Bookwalter, C.S.,Krementsova, E.B.,Moussaoui, D.,Previs, M.J.,Jousset, G.,Baum, J.,Trybus, K.M.,Houdusse, A. Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism. Nat Commun, 10:3286-3286, 2019 Cited by PubMed Abstract: Plasmodium parasites are obligate intracellular protozoa and causative agents of malaria, responsible for half a million deaths each year. The lifecycle progression of the parasite is reliant on cell motility, a process driven by myosin A, an unconventional single-headed class XIV molecular motor. Here we demonstrate that myosin A from Plasmodium falciparum (PfMyoA) is critical for red blood cell invasion. Further, using a combination of X-ray crystallography, kinetics, and in vitro motility assays, we elucidate the non-canonical interactions that drive this motor's function. We show that PfMyoA motor properties are tuned by heavy chain phosphorylation (Ser19), with unphosphorylated PfMyoA exhibiting enhanced ensemble force generation at the expense of speed. Regulated phosphorylation may therefore optimize PfMyoA for enhanced force generation during parasite invasion or for fast motility during dissemination. The three PfMyoA crystallographic structures presented here provide a blueprint for discovery of specific inhibitors designed to prevent parasite infection. PubMed: 31337750DOI: 10.1038/s41467-019-11120-0 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.82 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード