Figure 4.

High-Resolution 3D Structure of the DUS_var1-Recognizing ComP_sub

(A) Ribbon representation of the superposition of the ensemble of 20 ComP_sub structures determined by NMR.

(B) Cartoon representation of the ComP_sub structure. The conserved core in type IV pilins (the N-terminal α helix and four-stranded antiparallel β sheet) is depicted in gray. Distinctive/key structural features such as the α1β1 loop (red), the large β1-β2 loop (blue), and the DD region delimited by two disulfide bonds that sits on top of the β sheet (green) are also highlighted.

(C) Cartoon representation of the superposition of ComP_sub (magenta) and ComP (gray) structures. The two structures superpose with an rmsd of 2.41 Å over their entire length.