Binding of the motor protein SecA to the bacterial protein translocation channel SecYEG in the absence of ATP
K. Winkler, A. Karner, A. Horner, C. Hannesschlaeger, D. Knyazev, C. Siligan, M. Zimmermann, R. Kuttner, P. Pohl, J. Preiner
The paper investigates how SecA remains bound to SecYEG without ATP, showing stable interactions and conformational changes that support protein translocation.
Nanoscale Advances · Jan 1, 2020Peer-reviewedBiophysics