FtsZ
FtsZ, the first identified prokaryotic cytoskeletal element, forms a filamentous ring structure located in the middle of the cell called the Z-ring that constricts during cell division, similar to the actin-myosin contractile ring in eukaryotes. The Z-ring is a highly dynamic structure that consists of numerous bundles of protofilaments that extend and shrink, although the mechanism behind Z-ring contraction and the number of protofilaments involved are unclear. FtsZ acts as an organizer protein and is required for cell division. It is the first component of the septum during cytokinesis, and it recruits all other known cell division proteins to the division site.
Despite this functional similarity to actin, FtsZ is homologous to eukaryal tubulin. Although comparison of the primary structures of FtsZ and tubulin reveal a weak relationship, their 3-dimensional structures are remarkably similar. Furthermore, like tubulin, monomeric FtsZ is bound to GTP and polymerizes with other FtsZ monomers with the hydrolysis of GTP in a mechanism similar to tubulin dimerization. Since FtsZ is essential for cell division in bacteria, this protein is a target for the design of new antibiotics.
Read more about this topic: Prokaryotic Cytoskeleton