Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation
L. R. Kolich, Y.-T. Chang, N. Coudray, S. I. Giacometti, M. R. MacRae, G. L. Isom, E. M. Teran, G. Bhabha, D. C. Ekiert
The paper reports the X-ray structure of MlaFB from E. coli, revealing how the regulatory subunit MlaB stabilizes the nucleotide binding domain and how the C-terminal tail of MlaF mediates dimerization and complex assembly.
bioRxiv · Apr 27, 2020Microbiology