5LP4

Penicillin-Binding Protein (PBP2) from Helicobacter pylori

Summary for 5LP4

• Entry DOI: 10.2210/pdb5lp4/pdb
• Descriptor: Penicillin-binding protein 2 (Pbp2), SULFATE ION (3 entities in total)
• Functional Keywords: transferase, cell wall, hydrolase-antibiotic complex, hydrolase/antibiotic
• Biological source: Helicobacter pylori (strain ATCC 700392 / 26695)
• Total number of polymer chains: 2
• Total formula weight: 135721.91

Authors

Contreras-Martel, C.,Martins, A.,Ecobichon, C.,Maragno, D.M.,Mattei, P.J.,El Ghachi, M.,Boneca, I.G.,Dessen, A. (deposition date: 2016-08-11, release date: 2017-08-23, Last modification date: 2024-10-16)

Primary citation

Contreras-Martel, C.,Martins, A.,Ecobichon, C.,Trindade, D.M.,Mattei, P.J.,Hicham, S.,Hardouin, P.,Ghachi, M.E.,Boneca, I.G.,Dessen, A.
Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.
Nat Commun, 8:776-776, 2017

PubMed 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.Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth.

PubMed: 28974686
DOI: 10.1038/s41467-017-00783-2

Experimental method

X-RAY DIFFRACTION (3.03 Å)