Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex

Rie Nygaard, Chris L. B. Graham, Meagan Belcher Dufrisne, Jonathan D. Colburn, Joseph Pepe, Molly A. Hydorn, Silvia Corradi, Chelsea M. Brown, Khuram U. Ashraf, Owen N. Vickery, Nicholas S. Briggs, John J. Deering, Brian Kloss, Bruno Botta, Oliver B. Clarke, Linda Columbus (), Jonathan Dworkin (), Phillip J. Stansfeld (), David I. Roper () and Filippo Mancia ()
Additional contact information
Rie Nygaard: Columbia University Irving Medical Center
Chris L. B. Graham: University of Warwick
Meagan Belcher Dufrisne: University of Virginia
Jonathan D. Colburn: University of Warwick
Joseph Pepe: Columbia University Irving Medical Center
Molly A. Hydorn: Columbia University Irving Medical Center
Silvia Corradi: Columbia University Irving Medical Center
Chelsea M. Brown: University of Warwick
Khuram U. Ashraf: Columbia University Irving Medical Center
Owen N. Vickery: University of Warwick
Nicholas S. Briggs: University of Warwick
John J. Deering: University of Warwick
Brian Kloss: New York Structural Biology Center
Bruno Botta: Sapienza University of Rome
Oliver B. Clarke: Columbia University Irving Medical Center
Linda Columbus: University of Virginia
Jonathan Dworkin: Columbia University Irving Medical Center
Phillip J. Stansfeld: University of Warwick
David I. Roper: University of Warwick
Filippo Mancia: Columbia University Irving Medical Center

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-40483-8

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