4F1K

Crystal structure of the MG2+ free VWA domain of plasmodium falciparum trap protein

4F1K の概要

• エントリーDOI: 10.2210/pdb4f1k/pdb
• 関連するPDBエントリー: 4F1J
• 分子名称: Thrombospondin related anonymous protein, CHLORIDE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: rossmann fold, cell adhesion, dinucleotide binding, membrane
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46986.66

構造登録者

Pihlajamaa, T.,Knuuti, J.,Kajander, T.,Sharma, A.,Permi, P. (登録日: 2012-05-07, 公開日: 2013-01-30, 最終更新日: 2024-11-20)

主引用文献

Pihlajamaa, T.,Kajander, T.,Knuuti, J.,Horkka, K.,Sharma, A.,Permi, P.
Structure of Plasmodium falciparum TRAP (thrombospondin-related anonymous protein) A domain highlights distinct features in apicomplexan von Willebrand factor A homologues.
Biochem.J., 450:469-476, 2013

PubMed Abstract: TRAP (thrombospondin-related anonymous protein), localized in the micronemes and on the surface of sporozoites of the notorious malaria parasite Plasmodium, is a key molecule upon infection of mammalian host hepatocytes and invasion of mosquito salivary glands. TRAP contains two adhesive domains responsible for host cell recognition and invasion, and is known to be essential for infectivity. In the present paper, we report high-resolution crystal structures of the A domain of Plasmodium falciparum TRAP with and without bound Mg2+. The structure reveals a vWA (von Willebrand factor A)-like fold and a functional MIDAS (metal-ion-dependent adhesion site), as well as a potential heparan sulfate-binding site. Site-directed mutagenesis and cell-attachment assays were used to investigate the functional roles of the surface epitopes discovered. The reported structures are the first determined for a complete vWA domain of parasitic origin, highlighting unique features among homologous domains from other proteins characterized hitherto. Some of these are conserved among Plasmodiae exclusively, whereas others may be common to apicomplexan organisms in general.

PubMed: 23317521
DOI: 10.1042/BJ20121058

実験手法

X-RAY DIFFRACTION (1.87 Å)