ArticleJournal of structural biology2012
Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum.
Article in Journal of structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- The inner membrane complex protein, IMC55, is dispensable for intraerythrocytic development ofMicrobiology spectrum · 2026Article
- Identification of two genomic cryptotypes of Plasmodium malariae in Africa.PLoS neglected tropical diseases · 2026Article
- Identification of novel biomarkers for anti-Frontiers in microbiology · 2024Article
- Identification of Novel, Potent, and Selective Compounds against Malaria Using Glideosomal-Associated Protein 50 as a Drug Target.ACS omega · 2023Article
- Article
- Deciphering the Role of Protein Phosphatases in Apicomplexa: The Future of Innovative Therapeutics?Microorganisms · 2022Review
- Structural role of essential light chains in the apicomplexan glideosome.Communications biology · 2020Article
- The Dynamic Roles of the Inner Membrane Complex in the Multiple Stages of the Malaria Parasite.Frontiers in cellular and infection microbiology · 2020Review
- Disrupting assembly of the inner membrane complex blocks Plasmodium falciparum sexual stage development.PLoS pathogens · 2017Article
- The Plasmodium falciparum blood stages acquire factor H family proteins to evade destruction by human complement.Cellular microbiology · 2016Article
- Plant expression and characterization of the transmission-blocking vaccine candidate PfGAP50.BMC biotechnology · 2015Article
- Identification of Novel Ezrin Inhibitors Targeting Metastatic Osteosarcoma by Screening Open Access Malaria Box.Molecular cancer therapeutics · 2015Article
- Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Acta crystallographica. Section F, Structural biology communications · 2015Review
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
- The inner membrane complex through development of Toxoplasma gondii and Plasmodium.Cellular microbiology · 2014Review
- Development of a multifunctional tool for drug screening against plasmodial protein-protein interactions via surface plasmon resonance.Journal of molecular recognition : JMR · 2013Article
- Crystallization and preliminary structural characterization of the two actin isoforms of the malaria parasite.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- The compact conformation of the Plasmodium knowlesi myosin tail interacting protein MTIP in complex with the C-terminal helix of myosin A.Molecular and biochemical parasitology · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.