PDBsum entry 4f1j

Cell adhesion

PDB id: 4f1j

Contents

Protein chains

200 a.a.

Ligands

SO4 ×7

EDO ×12

Metals

_CL ×2

_MG ×4

Waters ×391

PDB id:

4f1j

Name:

Cell adhesion

Title:

Crystal structure of the mg2+ loaded vwa domain of plasmodium falciparum trap protein

Structure:

Thrombospondin related anonymous protein. Chain: a, b. Synonym: thrombospondin-related adhesive protein. Engineered: yes

Source:

Plasmodium falciparum. Organism_taxid: 5833. Gene: thrombospondin related anonymous protein (trap), trap. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.73Å R-factor: 0.179 R-free: 0.218

Authors:

T.Pihlajamaa,J.Knuuti,T.Kajander,A.Sharma,P.Permi

Key ref:

T.Pihlajamaa et al. (2013). 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. PubMed id: 23317521 DOI: 10.1042/BJ20121058

Date:

07-May-12 Release date: 30-Jan-13

Protein chains

Q01502  (Q01502_PLAFA) -  Thrombospondin related anonymous protein (Fragment) from Plasmodium falciparum

Seq: 559 a.a.

Struc: 200 a.a.

DOI no: 10.1042/BJ20121058

Biochem J 450:469-476 (2013)

PubMed id: 23317521

Structure of Plasmodium falciparum TRAP (thrombospondin-related anonymous protein) A domain highlights distinct features in apicomplexan von Willebrand factor A homologues.

T.Pihlajamaa, T.Kajander, J.Knuuti, K.Horkka, A.Sharma, P.Permi.

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.