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2QAC

The closed MTIP-MyosinA-tail complex from the malaria parasite invasion machinery

2QAC の概要
エントリーDOI10.2210/pdb2qac/pdb
関連するPDBエントリー2AUC
分子名称Myosin A tail domain interacting protein MTIP, Myosin-A (3 entities in total)
機能のキーワードmalaria invasion, structural genomics, psi, protein structure initiative, structural genomics of pathogenic protozoa consortium, sgpp, membrane protein
由来する生物種Plasmodium falciparum
詳細
細胞内の位置Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q7RQ71
タンパク質・核酸の鎖数2
化学式量合計18544.79
構造登録者
主引用文献Bosch, J.,Turley, S.,Roach, C.M.,Daly, T.M.,Bergman, L.W.,Hol, W.G.
The Closed MTIP-Myosin A-Tail Complex from the Malaria Parasite Invasion Machinery.
J.Mol.Biol., 372:77-88, 2007
Cited by
PubMed Abstract: The Myosin A-tail interacting protein (MTIP) of the malaria parasite links the actomyosin motor of the host cell invasion machinery to its inner membrane complex. We report here that at neutral pH Plasmodium falciparum MTIP in complex with Myosin A adopts a compact conformation, with its two domains completely surrounding the Myosin A-tail helix, dramatically different from previously observed extended MTIP structures. Crystallographic and mutagenesis studies show that H810 and K813 of Myosin A are key players in the formation of the compact MTIP:Myosin A complex. Only the unprotonated state of Myosin A-H810 is compatible with the compact complex. Most surprisingly, every side-chain atom of Myosin A-K813 is engaged in contacts with MTIP. While this side-chain was previously considered to prevent a compact conformation of MTIP with Myosin A, it actually appears to be essential for the formation of the compact complex. The hydrophobic pockets and adaptability seen in the available series of MTIP structures bodes well for the discovery of inhibitors of cell invasion by malaria parasites.
PubMed: 17628590
DOI: 10.1016/j.jmb.2007.06.016
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 2qac
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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