Proteomics

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Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii

ABSTRACT: The phylum of Apicomplexa groups intracellular parasites that employ substrate-dependent gliding motility to invade host cells, egress from the infected cells and cross biological barriers. The glideosome associated connector (GAC) is a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesins and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. Here, we present the crystal structure of Toxoplasma gondii GAC and reveal a unique, supercoiled armadillo repeat region that adopts a closed ring conformation. Characterisation of the membrane binding interface within the C-terminal PH domain as well as an N-terminal fragment necessary for association with F-actin suggest that GAC adopts multiple conformations. A multi-conformational model for assembly of GAC within the glideosome is proposed

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Toxoplasma Gondii Rh-88

SUBMITTER: Oscar Vadas  

LAB HEAD: Dominique Soldati-Favre

PROVIDER: PXD039335 | Pride | 2023-05-10

REPOSITORIES: Pride

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20221012_OV_HDXMS_100.raw Raw
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Publications

The phylum of Apicomplexa groups intracellular parasites that employ substrate-dependent gliding motility to invade host cells, egress from the infected cells, and cross biological barriers. The glideosome-associated connector (GAC) is a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesins and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. Here, we pre  ...[more]

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