Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain
G. Usluer, F. Dimaio, S. Yang, J. M. Hansen, J. K. Polka, R. D. Mullins, J. Kollman
The paper reports the cryo-EM structure of AlfA, a bacterial actin, revealing unique ATP-binding interactions and a missing subdomain that explain its distinct assembly dynamics and plasmid segregation function.
bioRxiv · Sep 7, 2017Biophysics