The utilization of organized supramolecular assemblies to exploit the synergistic interactions afforded by close proximity, both for enzymatic synthesis and for the degradation of recalcitrant substrates, is an emerging theme in cellular biology. Anaerobic bacteria harness a multiprotein complex, termed the “cellulosome,” for efficient degradation of the plant cell wall. This megadalton catalytic machine organizes an enzymatic consortium on a multifaceted molecular scaffold whose “cohesin” domains interact with corresponding “dockerin” domains of the enzymes. Here we report the structure of the cohesin–dockerin complex from Clostridium thermocellum at 2.2-Å resolution. The data show that the β-sheet cohesin domain interacts predominantly with one of the helices of the dockerin. Whereas the structure of the cohesin remains essentially unchanged, the loop–helix–helix–loop–helix motif of the dockerin undergoes conformational change and ordering compared with its solution structure, although the classical 12-residue EF-hand coordination to two calcium ions is maintained. Significantly, internal sequence duplication within the dockerin is manifested in near-perfect internal twofold symmetry, suggesting that both “halves” of the dockerin may interact with cohesins in a similar manner, thus providing a higher level of structure to the cellulosome and possibly explaining the presence of “polycellulosomes.” The structure provides an explanation for the lack of cross-species recognition between cohesin–dockerin pairs and thus provides a blueprint for the rational design, construction, and exploitation of these catalytic assemblies.

Spirulina (Limnospira platensis) is a microalga recognised for its rich nutritional composition and diverse bioactive compounds, making it a valuable functional food, feed, and therapeutic agent. This review examines spirulina’s chemical composition, including its high levels of protein, essential fatty acids, vitamins, minerals, and bioactive compounds, such as the phycocyanin pigment, polysaccharides, and carotenoids, in food, feed, and medicine. These compounds exhibit various biological activities, including antioxidant, anti-inflammatory, immunomodulatory, antiviral, anticancer, antidiabetic and lipid-lowering effects. Spirulina’s potential to mitigate oxidative stress, enhance immune function, and inhibit tumour growth positions it as a promising candidate for preventing chronic diseases. Additionally, spirulina is gaining interest in the animal feed sector as a promotor of growth performance, improving immune responses and increasing resistance to diseases in livestock, poultry, and aquaculture. Despite its well-documented health benefits, future research is needed to optimize production/cultivation methods, improve its bioavailability, and validate its efficacy (dose–effect relationship) and safety through clinical trials and large-scale human trials. This review underscores the potential of spirulina to address global health and nutrition challenges, supporting its continued application in food, feed, and medicine.

The assembly of proteins that display complementary activities into macromolecular complexes is critical to cellular function. One such enzyme complex, of environmental significance, is the plant cell wall degrading apparatus of anaerobic bacteria, termed the cellulosome. The complex assembles through the interaction of enzyme-derived “type I dockerin” modules with the multiple “cohesin” modules of the scaffolding protein. Clostridium thermocellum type I dockerin modules contain a duplicated 22-residue sequence that comprises helix-1 and helix-3, respectively. The crystal structure of a C. thermocellum type I cohesin-dockerin complex showed that cohesin recognition was predominantly through helix-3 of the dockerin. The sequence duplication is reflected in near-perfect 2-fold structural symmetry, suggesting that both repeats could interact with cohesins by a common mechanism in wild-type (WT) proteins. Here, a helix-3 disrupted mutant dockerin is used to visualize the reverse binding in which the dockerin mutant is indeed rotated 180° relative to the WT dockerin such that helix-1 now dominates recognition of its protein partner. The dual binding mode is predicted to impart significant plasticity into the orientation of the catalytic subunits within this supramolecular assembly, which reflects the challenges presented by the degradation of a heterogeneous, recalcitrant, insoluble substrate by a tethered macromolecular complex.