Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex

Carlos Contreras-Martel, Alexandre Martins, Chantal Ecobichon, Daniel Maragno Trindade, Pierre-Jean Matteï, Samia Hicham, Pierre Hardouin, Meriem El Ghachi, Ivo G. Boneca () and Andréa Dessen ()
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Carlos Contreras-Martel: Bacterial Pathogenesis Group
Alexandre Martins: Bacterial Pathogenesis Group
Chantal Ecobichon: Unit of Biology and Genetics of the Bacterial Cell Wall
Daniel Maragno Trindade: CNPEM, Campinas
Pierre-Jean Matteï: Bacterial Pathogenesis Group
Samia Hicham: Unit of Biology and Genetics of the Bacterial Cell Wall
Pierre Hardouin: Bacterial Pathogenesis Group
Meriem El Ghachi: Unit of Biology and Genetics of the Bacterial Cell Wall
Ivo G. Boneca: Unit of Biology and Genetics of the Bacterial Cell Wall
Andréa Dessen: Bacterial Pathogenesis Group

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the “divisome”) and lateral wall growth (the “elongasome”). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2:MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2:MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors.

Date: 2017
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DOI: 10.1038/s41467-017-00783-2

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