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Sayuri sugawara open the gate rare5/4/2023 These properties make Triplin perhaps the most complex pore-forming molecular machine described to date. All results support the hypothesis that one of the three subunits is oriented in a direction opposite to that of the other two. Theoretical calculations indicate that the charge on the voltage sensor can explain the rectification of the current flowing through the open pores if it is located near the pore mouth in the open state. A mechanism underlying the cooperativity was also identified. From asymmetrical addition of these reagents, the positively charged voltage sensors translocate across the membrane and are, thus, responsible energetically for the steep voltage dependence. Trypsin cleavage of the sensor eliminates voltage gating by cleaving the sensor. By using chemical modification to reduce the charge on the voltage sensors, they were shown to be positively charged structures. We report detailed insights into the molecular basis for these very unusual properties explored at the single-molecule level. A similar trimeric channel former, named Triplin, displays very steep voltage dependence, rivaling that responsible for the electrical excitability of mammals, and high inter-subunit cooperativity. Gram-negative bacteria have a large variety of channel-forming proteins in their outer membrane, generally referred to as porins.
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