Chaperonins are key components of the cell machinery and are involved in the productive folding of proteins. Most chaperonins share a common general morphology based in a cylinder composed of two rings of 7-9 subunits, with a conspicuous cavity inside the particle. Chaperonins have been classified into two groups according to their sequence homologies: type I, whose better known member is GroEL, and type II comprising the eukaryotic cytosolic CCT and the archaebacterial thermosome, among others. Although the basic structure of both chaperonin types is rather similar, there are a number of basic differences among them. Whereas GroEL is rather non-specific regarding its substrate, CCT is more specialized, and plays a fundamental role in the folding of cytoskeletal proteins. Another important difference is that GroEL is an homopolymer, while CCT is an heteromeric complex built up of eight different polypeptides. Furthermore, GroEL requires a cofactor (GroES) that is not present in the type II chaperonins.
Recent studies of the structure of CCT have allowed a deeper insight into its function. Electron microscopic analyses have revealed a different behavior of this chaperonin after binding to nucleotides, respect to GroEL. The atomic structure of the thermosome fits into the electron microscopy reconstructed volume of the CCT. This fitting gives clues to compare the structural transitions of GroEL and CCT during the folding cycle. The different changes undergone by the two chaperonins suggest the existence of differences in the way they bind substrates and enlarge the internal cavity, as well as a different type of signaling between the two rings of the types I and II chaperonins.