2AUC

Structure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motor

Summary for 2AUC

• Entry DOI: 10.2210/pdb2auc/pdb
• Descriptor: Myosin A Tail Interacting Protein, Myosin A (3 entities in total)
• Functional Keywords: sgpp, structural genomics, psi, protein structure initiative mtip, myoa, myosin a-tail, myoa tail interacting protein, structural genomics of pathogenic protozoa consortium, membrane protein
• Biological source: Plasmodium knowlesi; More
• Total number of polymer chains: 4
• Total formula weight: 46281.35

Authors

Bosch, J.,Turley, S.,Hol, W.G.J.,Structural Genomics of Pathogenic Protozoa Consortium (SGPP) (deposition date: 2005-08-27, release date: 2006-01-17, Last modification date: 2025-03-26)

Primary citation

Bosch, J.,Turley, S.,Daly, T.M.,Bogh, S.M.,Villasmil, M.L.,Roach, C.,Zhou, N.,Morrisey, J.M.,Vaidya, A.B.,Bergman, L.W.,Hol, W.G.
Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor.
Proc.Natl.Acad.Sci.Usa, 103:4852-4857, 2006

PubMed Abstract: The causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials.

PubMed: 16547135
DOI: 10.1073/pnas.0510907103

Experimental method

X-RAY DIFFRACTION (2.6 Å)