Cohesin-dockerin interaction cellulosome

In general, two major types of subunit compose cellulosomes the noncatalytic scaffoldin(s) and the catalyticahy active components. Each of these structures may be quite complex. The assembly of the cehulosome is facilitated by the high-affinity recognition between the scaffoldin cohesin and the enzymes dockerin modules. The scaffoldin often contains multiple cohesin modules, thereby enabling numerous different enzymes to be assembled into the cehulosome complex. In addition, in some species, such as Acetivibrio cellulolyticus, the cellulosomes present multiple scaffoldins with different cohesins [41]. The interaction cohesin-dockerins is type and specie-specific. 

Within the cellulosome complex, type I dockerin domain is responsible for incorporating its associated glycosyl hydrolase in the bacterial cellulosome via interaction with a reception domain, the cohesin domain. The three-dimensional solution structure of the 69-residue dockerin domain from the thermophilic Clostridium thermocellum (Topt = 55-65 °C) was solved by NMR and was found to consist of two Ca " -binding loop-helix motifs connected by a linker. Each Ca " -binding subdomain is stabilized by a cluster of buried hydrophobic sidechains. Recently, the NMR sequence-specific resonance assignment of type II cohesin module from C. thermocellum has been published. ... 

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