 The phylum of apocomplexa contains intracellular parasites that use substrate-dependent gliding motility to invade host cells, egress from the infected cells, and cross biological barriers. This process requires the Glideosome Associated Connector, GAC, which is composed of a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesions and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. New research has revealed the structure of toxoplasma gondii GAC, which consists of a supercoiled armadillo repeat region that adopts a closed ring conformation. This structure provides insight into how GAC assembles and regulates itself within the Glideosome, allowing it to perform its crucial role in the invasion process. This article was authored by Amit Kumar, Oscar Vedas, Nicholas Dos Santos Pacheco, and others.