Journal article
The Closed MTIP-Myosin A-Tail Complex from the Malaria Parasite Invasion Machinery
Journal of molecular biology, v 372(1), pp 77-88
2007
PMID: 17628590
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The Myosin A-tail interacting protein (MTIP) of the malaria parasite links the actomyosin motor of the host cell invasion machinery to its inner membrane complex. We report here that at neutral pH
Plasmodium falciparum MTIP in complex with Myosin A adopts a compact conformation, with its two domains completely surrounding the Myosin A-tail helix, dramatically different from previously observed extended MTIP structures. Crystallographic and mutagenesis studies show that H810 and K813 of Myosin A are key players in the formation of the compact MTIP:Myosin A complex. Only the unprotonated state of Myosin A-H810 is compatible with the compact complex. Most surprisingly, every side-chain atom of Myosin A-K813 is engaged in contacts with MTIP. While this side-chain was previously considered to prevent a compact conformation of MTIP with Myosin A, it actually appears to be essential for the formation of the compact complex. The hydrophobic pockets and adaptability seen in the available series of MTIP structures bodes well for the discovery of inhibitors of cell invasion by malaria parasites.
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Details
- Title
- The Closed MTIP-Myosin A-Tail Complex from the Malaria Parasite Invasion Machinery
- Creators
- Jürgen Bosch - Department of Biochemistry, University of Washington, Seattle, WA 98195, USAStewart Turley - Department of Biochemistry, University of Washington, Seattle, WA 98195, USAClaudia M Roach - Department of Biochemistry, University of Washington, Seattle, WA 98195, USAThomas M Daly - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, USALawrence W Bergman - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, USAWim G.J Hol - Department of Biochemistry, University of Washington, Seattle, WA 98195, USA
- Publication Details
- Journal of molecular biology, v 372(1), pp 77-88
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology; [Retired Faculty]
- Web of Science ID
- WOS:000249274100008
- Scopus ID
- 2-s2.0-34547682065
- Other Identifier
- 991014877706304721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology