Journal article
Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum
Journal of structural biology, v 178(1)
Apr 2012
PMID: 22387043
Featured in Collection : UN Sustainable Development Goals @ Drexel
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 Co2+ ions of 18Å.
Metrics
Details
- Title
- Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum
- Creators
- Jürgen Bosch - Departments of Biochemistry and Biological Structure, Biomolecular Structure Center, University of Washington, Seattle, WA 98195, United StatesMatthew H Paige - Departments of Biochemistry and Biological Structure, Biomolecular Structure Center, University of Washington, Seattle, WA 98195, United StatesAkhil B Vaidya - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, United StatesLawrence W Bergman - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, United StatesWim G.J Hol - Departments of Biochemistry and Biological Structure, Biomolecular Structure Center, University of Washington, Seattle, WA 98195, United States
- Publication Details
- Journal of structural biology, v 178(1)
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology; [Retired Faculty]
- Web of Science ID
- WOS:000302977400008
- Scopus ID
- 2-s2.0-84859431587
- Other Identifier
- 991014878233004721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics
- Cell Biology