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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii Amit Kumar , Oscar Vadas , Nicolas Dos Santos Pacheco , Xu Zhang , Kin Chao , Nicolas Darvill , Helena Ø. Rasmussen , Yingqi Xu , Gloria Meng-Hsuan Lin , Fisentzos A. Stylianou , Jan Skov Pedersen , Sarah L. Rouse , Marc L. Morgan , Dominique Soldati-Favre , Stephen Matthews Elife 12 DOI: 10.7554/eLife.86049 Diamond Proposal Number(s): [23620] Open Access Show Abstract ▼ 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 solution properties together with membrane and F-actin binding interfaces suggests that GAC adopts several conformations from closed to open and extended. A multi-conformational model for assembly and regulation of GAC within the glideosome is proposed.	Apr 2023
I04-Macromolecular Crystallography	Secondary structure and X-ray crystallographic analysis of the glideosome-associated connector (GAC) from Toxoplasma gondii Amit Kumar , Xu Zhang , Oscar Vadas , Fisentzos A. Stylianou , Nicolas Dos Santos Pacheco , Sarah L. Rouse , Marc L. Morgan , Dominique Soldati-Favre , Steve Matthews Crystals 12 DOI: 10.3390/cryst12010110 Open Access Show Abstract ▼ Abstract: A model for parasitic motility has been proposed in which parasite filamentous actin (F-actin) is attached to surface adhesins by a large component of the glideosome, known as the glideosome-associated connector protein (GAC). This large 286 kDa protein interacts at the cytoplasmic face of the plasma membrane with the phosphatidic acid-enriched inner leaflet and cytosolic tails of surface adhesins to connect them to the parasite actomyosin system. GAC is observed initially to the conoid at the apical pole and re-localised with the glideosome to the basal pole in gliding parasite. GAC presumably functions in force transmission to surface adhesins in the plasma membrane and not in force generation. Proper connection between F-actin and the adhesins is as important for motility and invasion as motor operation itself. This notion highlights the need for new structural information on GAC interactions, which has eluded the field since its discovery. We have obtained crystals that diffracted to 2.6–2.9 Å for full-length GAC from Toxoplasma gondii in native and selenomethionine-labelled forms. These crystals belong to space group P212121; cell dimensions are roughly a = 119 Å, b = 123 Å, c = 221 Å, α = 90°, β = 90° and γ = 90° with 1 molecule per asymmetric unit, suggesting a more compact conformation than previously proposed.	Jan 2022

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