5OUP

Structure of TgPLP1 MACPF domain

5OUP の概要

• エントリーDOI: 10.2210/pdb5oup/pdb
• 分子名称: Perforin-like protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: toxoplasma, cell egress, macpf domain, lipid binding protein
• 由来する生物種: Toxoplasma gondii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39333.93

構造登録者

Ni, T.,Gilbert, R.J.C. (登録日: 2017-08-24, 公開日: 2018-04-11, 最終更新日: 2024-11-13)

主引用文献

Ni, T.,Williams, S.I.,Rezelj, S.,Anderluh, G.,Harlos, K.,Stansfeld, P.J.,Gilbert, R.J.C.
Structures of monomeric and oligomeric forms of theToxoplasma gondiiperforin-like protein 1.
Sci Adv, 4:eaaq0762-eaaq0762, 2018

PubMed Abstract: and are the parasitic agents of toxoplasmosis and malaria, respectively, and use perforin-like proteins (PLPs) to invade host organisms and complete their life cycles. The PLP1 (PLP1) is required for efficient exit from parasitophorous vacuoles in which proliferation occurs. We report structures of the membrane attack complex/perforin (MACPF) and Apicomplexan PLP C-terminal β-pleated sheet (APCβ) domains of PLP1. The MACPF domain forms hexameric assemblies, with ring and helix geometries, and the APCβ domain has a novel β-prism fold joined to the MACPF domain by a short linker. Molecular dynamics simulations suggest that the helical MACPF oligomer preserves a biologically important interface, whereas the APCβ domain binds preferentially through a hydrophobic loop to membrane phosphatidylethanolamine, enhanced by the additional presence of inositol phosphate lipids. This mode of membrane binding is supported by site-directed mutagenesis data from a liposome-based assay. Together, these structural and biophysical findings provide insights into the molecular mechanism of membrane targeting by PLP1.

PubMed: 29750191
DOI: 10.1126/sciadv.aaq0762

実験手法

X-RAY DIFFRACTION (2.03 Å)