N-terminal domain of Myosin essential light chain ELC
ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.
Structure:6ZN3_A: Plasmodium falciparum trimeric glideosome sub-complex of PfELC with MyoA and MLC1/MTIP; contacts at 4A.
Comment:The apicomplexan glideosome is composed of six proteins: myosin MyoA, essential light chain ELC, myosin light chain MLC1/MTIP, and the glideosome-associated proteins GAP40, GAP45 and GAP50.
Jiyao W et al.(2023). "The conserved domain database in 2023.",