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

Jürgen Bosch; Stewart Turley; Thomas M. Daly; Stephen M. Bogh; Michelle L. Villasmil; Claudia Roach; Na Zhou; Joanne M. Morrisey; Akhil B. Vaidya; Lawrence W. Bergman; Wim G J Hol

doi:10.1073/pnas.0510907103

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

Jürgen Bosch, Stewart Turley, Thomas M. Daly, Stephen M. Bogh, Michelle L. Villasmil, Claudia Roach, Na Zhou, Joanne M. Morrisey, Akhil B. Vaidya, Lawrence W. Bergman, Wim G J Hol

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	4852-4857
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	103
Issue number	13
DOIs	https://doi.org/10.1073/pnas.0510907103
State	Published - Mar 28 2006
Externally published	Yes

Keywords

Cell invasion machinery
Gliding motility
Myosin-tail-interacting protein
Plasmodium

ASJC Scopus subject areas

Genetics
General

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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. J. (2006). Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor. Proceedings of the National Academy of Sciences of the United States of America, 103(13), 4852-4857. https://doi.org/10.1073/pnas.0510907103

Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor. / Bosch, Jürgen; Turley, Stewart; Daly, Thomas M.; Bogh, Stephen M.; Villasmil, Michelle L.; Roach, Claudia; Zhou, Na; Morrisey, Joanne M.; Vaidya, Akhil B.; Bergman, Lawrence W.; Hol, Wim G J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, No. 13, 28.03.2006, p. 4852-4857.

Research output: Contribution to journal › Article › peer-review

Bosch, J, Turley, S, Daly, TM, Bogh, SM, Villasmil, ML, Roach, C, Zhou, N, Morrisey, JM, Vaidya, AB, Bergman, LW & Hol, WGJ 2006, 'Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor', Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 13, pp. 4852-4857. https://doi.org/10.1073/pnas.0510907103

Bosch, Jürgen ; Turley, Stewart ; Daly, Thomas M. ; Bogh, Stephen M. ; Villasmil, Michelle L. ; Roach, Claudia ; Zhou, Na ; Morrisey, Joanne M. ; Vaidya, Akhil B. ; Bergman, Lawrence W. ; Hol, Wim G J. / Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor. In: Proceedings of the National Academy of Sciences of the United States of America. 2006 ; Vol. 103, No. 13. pp. 4852-4857.

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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.",

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AU - Villasmil, Michelle L.

AU - Roach, Claudia

AU - Zhou, Na

AU - Morrisey, Joanne M.

AU - Vaidya, Akhil B.

AU - Bergman, Lawrence W.

AU - Hol, Wim G J

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AB - 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.

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KW - Gliding motility

KW - Myosin-tail-interacting protein

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

Abstract

Keywords

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