Fig. 3: RctB domain IV structure reveals two dimerization interface involved in 29/39m-mediated inhibition.
a Crystal structure of the RctBIV dimer. Each monomer is composed of an αβ N-terminal subdomain (dark blue) connected to a four α-helices bundle (light blue) via a hinge region. b Topological representation of RctBIV dimer. The primary dimer interface (blue shadow) is formed by the extension of the central β-sheet of each monomer through β3 and the antiparallel interactions of the stacking α1. c Crystallographic tetramer formed through lattice contacts mediated by the C-terminal subdomain of neighboring dimers. Important residues contributing to the primary interface are shown in dark green. The secondary interface (yellow shadow) with the I625 and L651 functionally relevant residues shown in red. d 2D class averages of RctB obtained from cryo-EM e Bacterial-Two-hybrid of RctB-D314P vs. RctB domain IV mutants. Empty (negative control), Zip (positive control). Blue colonies indicate a positive protein-protein interaction, while white colonies indicate no interaction. Any blue dots within white colonies are due to lacZ+ revertant and should not be considered as evidence of interaction. f ChIP-seq of the RctB-L651P mutant at ori2. Same legend as for Fig. 2a.
