Viral connectors are key components of the life cycle of bacteriophages and other viral systems. They participate in procapsid assembly, and they are instrumental in DNA packaging and release. Connector proteins build hollow cylindrical dodecamers that show an overall morphological similarity among different viral systems including a remarkable conserved domain in the central part of the protein. These domains build the wall of the channel forming a 24 α-helices stretch together with an α-β extension. A similar α-helical arrangement is found in other unspecific DNA translocating complexes, suggesting the existence of a common structural signature for channel formation. Preliminary experiments suggest that connectors might be ideal candidates as nanopores for synthetic applications in nanotechnology.