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- Title
Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.
- Authors
Nygaard, Rie; Graham, Chris L. B.; Belcher Dufrisne, Meagan; Colburn, Jonathan D.; Pepe, Joseph; Hydorn, Molly A.; Corradi, Silvia; Brown, Chelsea M.; Ashraf, Khuram U.; Vickery, Owen N.; Briggs, Nicholas S.; Deering, John J.; Kloss, Brian; Botta, Bruno; Clarke, Oliver B.; Columbus, Linda; Dworkin, Jonathan; Stansfeld, Phillip J.; Roper, David I.; Mancia, Filippo
- Abstract
Peptidoglycan (PG) is an essential structural component of the bacterial cell wall that is synthetized during cell division and elongation. PG forms an extracellular polymer crucial for cellular viability, the synthesis of which is the target of many antibiotics. PG assembly requires a glycosyltransferase (GT) to generate a glycan polymer using a Lipid II substrate, which is then crosslinked to the existing PG via a transpeptidase (TP) reaction. A Shape, Elongation, Division and Sporulation (SEDS) GT enzyme and a Class B Penicillin Binding Protein (PBP) form the core of the multi-protein complex required for PG assembly. Here we used single particle cryo-electron microscopy to determine the structure of a cell elongation-specific E. coli RodA-PBP2 complex. We combine this information with biochemical, genetic, spectroscopic, and computational analyses to identify the Lipid II binding sites and propose a mechanism for Lipid II polymerization. Our data suggest a hypothesis for the movement of the glycan strand from the Lipid II polymerization site of RodA towards the TP site of PBP2, functionally linking these two central enzymatic activities required for cell wall peptidoglycan biosynthesis. Bacterial cell shape is dependent on the formation of the extracellular sugar polymer called peptidoglycan. Here the authors describe RodA-PBP2, the enzymatic core of the elongasome, which is the complex responsible peptidoglycan synthesis, and utilize an integrated approach to investigate the mechanism of peptidoglycan biosynthesis.
- Subjects
ESCHERICHIA coli; CELL morphology; BINDING sites; CELL anatomy; CARRIER proteins; GLYCANS; BACTERIAL cell walls
- Publication
Nature Communications, 2023, Vol 14, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-023-40483-8