4F1J

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

Summary for 4F1J

• Entry DOI: 10.2210/pdb4f1j/pdb
• Related: 4F1K
• Descriptor: Thrombospondin related anonymous protein, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: rossmann fold, cell adhesion, dinucleotide binding, membrane
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 2
• Total formula weight: 47117.87

Authors

Pihlajamaa, T.,Knuuti, J.,Kajander, T.,Sharma, A.,Permi, P. (deposition date: 2012-05-07, release date: 2013-01-30, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.73 Å)