One ring (or two) to hold them all - on the structure and function of protein nanotubes

摘要: Understanding the structural determinants relevant to formation of supramolecular assemblies homo-oligomeric proteins is a traditional and central scope biology. The knowledge thus gained crucial both infer their physiological function exploit architecture for bionanomaterials design. Protein nanotubes made by one-dimensional arrays homo-oligomers can be generated either commutative mechanism, yielding an 'open' structure (e.g. actin), or noncommutative whereby final formed hierarchical self-assembly intermediate 'closed' structures. Examples latter process are poorly described rules which they assemble have not been unequivocally defined. We collected investigated examples circular arrangements that form filaments stacked rings mechanism in vivo vitro. Based on quaternary structure, protein subunits subdivided into two groups we term Rings Dimers peroxiredoxin stable 1) thermosome/rosettasome), depending sub-structures identified within assembly (and, some cases, populated solution under selected experimental conditions). Structural analysis allowed us identify ring-like molecular chaperones filamentous-like formulate novel hypothesis nanotube assembly, chaperone activity macromolecular crowding may interconnected.