AbstractNot only eukaryotes, but also prokaryotes possess a cytoskeleton. Tubulin‐related bacterial protein FtsZ, and actin‐related bacterial proteins MreB/Mbl have recently been described as constituents of bacterial cytoskeletons. Genes coding for MreB/Mbl could only be found in elongated bacteria, not in coccoid forms. It was speculated that constituents of today's eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.Prior to the description of proteins MreB/Mbl, evidence had been obtained for the existence of a shape‐preserving cytoskeleton ubiquitously present in all bacteria. In the meantime, structural studies allow to speculate on a possible role of bacterial elongation factor Tu (EF‐Tu) as a structural element in such a “cytoskeletal web”. EF‐Tu was long known to form fibrillar structures in vitro; now experimental data accumulate, pointing towards formation of intracellular protofilaments containing EF‐Tu, and networks thereof as well. In addition, results of these structural studies suggest a so far unknown mode of complex formation of EF‐Tu with active ribosomes: ribosomes/polysomes were seen to be attached to intracellular protofilaments. Implications for the understanding of EF‐Tu—ribosome interaction, and a role of such a kind of putative protofilaments as a general site of attachment for cellular functional macromolecules are discussed. The notion is discussed that an EF‐Tu‐containing cytoskeletal web might have been the “primary” or “basic” kind of prokaryotic cytoskeleton, already in existence prior to the “invention” of precursors of today's MreB.