Contractile injection programs (CISs) [type VI secretion system (T6SS), phage tails, and tailocins] use a contractile sheath-rigid tube equipment to breach cell partitions and lipid membranes. The buildings of the pre- and postcontraction states of a number of CISs are recognized, however the mechanism of contraction stays poorly understood. Combining structural data of the top states of the 12-megadalton R-type pyocin sheath-tube advanced with thermodynamic and pressure spectroscopy analyses and an authentic modeling process, we describe the mechanism of pyocin contraction. We present that this nanomachine has an activation power of 160 kilocalories/mole (kcal/mol), and it releases 2160 kcal/mol of warmth and develops a pressure higher than 500 piconewtons. Our mixed strategy gives a quantitative and experimental description of the membrane penetration course of by a CIS.
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