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• W1968810931 abstract "Flagellar motors embedded in bacterial membranes are molecular machines powered by specific ion flows. Each motor is composed of a stator and a rotor and the interactions of those components are believed to generate the torque. Na(+) influx through the PomA/PomB stator complex of Vibrio alginolyticus is coupled to torque generation and is speculated to trigger structural changes in the cytoplasmic domain of PomA that interacts with a rotor protein in the C-ring, FliG, to drive the rotation. In this study, we tried to overproduce the cytoplasmic loop of PomA (PomA-Loop), but it was insoluble. Thus, we made a fusion protein with a small soluble tag (GB1) which allowed us to express and characterize the recombinant protein. The structure of the PomA-Loop seems to be very elongated or has a loose tertiary structure. When the PomA-Loop protein was produced in E. coli, a slight dominant effect was observed on motility. We conclude that the cytoplasmic loop alone retains a certain function." @default.
• W1968810931 created "2016-06-24" @default.
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• W1968810931 date "2013-01-01" @default.
• W1968810931 modified "2023-09-28" @default.
• W1968810931 title "Expression, purification and biochemical characterization of the cytoplasmic loop of PomA, a stator component of the Na⁺ driven flagellar motor" @default.
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• W1968810931 doi "https://doi.org/10.2142/biophysics.9.21" @default.
• W1968810931 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4629686" @default.
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• W1968810931 hasPublicationYear "2013" @default.
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