3TGH

GAP50 the anchor in the inner membrane complex of Plasmodium

Summary for 3TGH

• Entry DOI: 10.2210/pdb3tgh/pdb
• Descriptor: Glideosome-associated protein 50, SULFATE ION, COBALT (II) ION, ... (5 entities in total)
• Functional Keywords: phosphatase fold, not a phosphatase, motor protein, structural protein, membrane protein, cell invasion
• Biological source: Plasmodium falciparum 3D7
• Total number of polymer chains: 1
• Total formula weight: 38978.78

Authors

Bosch, J.,Paige, M.H.,Vaidya, A.,Bergman, L.,Hol, W.G.J. (deposition date: 2011-08-17, release date: 2012-03-07, Last modification date: 2023-09-13)

Primary citation

Bosch, J.,Paige, M.H.,Vaidya, A.B.,Bergman, L.W.,Hol, W.G.
Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum.
J.Struct.Biol., 178:61-73, 2012

PubMed Abstract: The glideosome associated protein GAP50 is an essential protein in apicomplexan parasites such as Plasmodium, Toxoplasma and Cryptosporidium, several species of which are important human pathogens. The 44.6kDa protein is part of a multi-protein complex known as the invasion machinery or glideosome, which is required for cell invasion and substrate gliding motility empowered by an actin-myosin motor. GAP50 is anchored through its C-terminal transmembrane helix into the inner membrane complex and interacts via a short six residue C-terminal tail with other proteins of the invasion machinery in the pellicle of the parasite. In this paper we describe the 1.7Å resolution crystal structure of the soluble GAP50 domain from the malaria parasite Plasmodium falciparum. The structure shows an αßßα fold with overall similarity to purple acid phosphatases with, however, little homology regarding the nature of the residues in the active site region of the latter enzyme. While purple acid phosphatases contain a phosphate bridged binuclear Fe-site coordinated by seven side chains with the Fe-ions 3.2Å apart, GAP50 in our crystals contains two cobalt ions each with one protein ligand and a distance between the Co(2+) ions of 18Å.

PubMed: 22387043
DOI: 10.1016/j.jsb.2012.02.009

Experimental method

X-RAY DIFFRACTION (1.7 Å)