Abstract

The architectural elements of four protein cages (bacterio ferritin, human mitochondrial ferritin, sulfur oxygenase reductase and small heat-shock protein) are compared top-to-bottom. The starting points are polyhedra with octahedral symmetry 432 enclosing the cage and delimiting the central cavity, respectively, which have vertices at points of a species-dependent cubic form lattice. The approach is extended from the whole cage to axial-symmetric clusters down to polyhedral forms of single monomers viewed along the fourfold, the threefold and the twofold axes, respectively. The corresponding projected monomeric forms can be approximated by two-dimensional tiles, 13 enantiomorphic pairs in total. The determination of the cubic indices of the monomeric vertices opens the possibility of the way back analysis, bottom-to-top, as discussed in paper II [Janner (2008). Acta Cryst. A64, 503-512].

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