8TJ3

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

Summary for 8TJ3

• Entry DOI: 10.2210/pdb8tj3/pdb
• EMDB information: 41299
• Descriptor: Peptidoglycan glycosyltransferase MrdB, Peptidoglycan D,D-transpeptidase MrdA (2 entities in total)
• Functional Keywords: peptidoglycan, glycosyltransferase, enzyme, membrane protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 111452.18

Authors

Nygaard, R.,Mancia, F. (deposition date: 2023-07-20, release date: 2023-08-30, Last modification date: 2024-05-01)

Primary citation

Nygaard, R.,Graham, C.L.B.,Belcher Dufrisne, M.,Colburn, J.D.,Pepe, J.,Hydorn, M.A.,Corradi, S.,Brown, C.M.,Ashraf, K.U.,Vickery, O.N.,Briggs, N.S.,Deering, J.J.,Kloss, B.,Botta, B.,Clarke, O.B.,Columbus, L.,Dworkin, J.,Stansfeld, P.J.,Roper, D.I.,Mancia, F.
Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.
Nat Commun, 14:5151-5151, 2023

PubMed 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.

PubMed: 37620344
DOI: 10.1038/s41467-023-40483-8

Experimental method

ELECTRON MICROSCOPY (3.2 Å)