Fig. 3
From: Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC
Remodeling of McrBΔN by McrC. a The dimer of McrC (ribbon representation) in complex with McrB∆N hexamer (surface representation). Note that this view looks at the face of the ring opposite to that in Fig. 1d. b The structure of an McrC monomer with the nuclease catalytic residues highlighted. c The asymmetric interaction of a monomer of McrC with McrB∆N hexamer. For clarity, protomer E of McrB∆N has been hidden. d Structure of McrB∆NC with the pore of the ring blocked by McrC is shown in the center. Around this figure, the interactions between McrC and the six McrB∆N protomers are illustrated. The inset is a zoom of the interactions between the helix bundle of McrC and L3 and C-terminal domain of McrB∆N protomers, highlighting the McrC-mediated remodeling of L3 in subunits A, B, C and D. The side chains of L3 residues are colored differently. Note the change in position of McrB-V341 (turquoise) and McrB-L339 (green), marked in dashed circles. The steric interaction between the helix bundle of McrC and L3 of B and C subunits are indicated by arrows (gray)
