Fig. 2
From: Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex
MreC binding engenders opening of the N-terminus of PBP2. a Overlay of MreC-bound and unbound PBP2 structures, indicating movement of the anchor region (in red). Opening of the N-terminal region of PBP2 exposes a hydrophobic region on the head that is complemented by a non-polar face on the surface of MreC (b), forming a hydrophobic zipper whose disruption hinders complex formation. c Structure-based sequence alignment between class B PBPs from H. pylori (this work), P. aeruginosa PAO1 G3XCV7, E. coli O157:H7 P0AD67, and K. pneumoniae A0A0W8ASI8 (UniProt codes). Head, anchor, linker, and TP are indicated in color above the sequence. Residues involved in interaction between head and anchor are indicated with black asterisks. Active site residues are indicated with hash tags. Figure generated with ESPRIPT53
