9DVC

Thermus thermophilus MreC-MreD complex with a C-terminal MreD BRIL fusion and an anti-BRIL Fab

Summary for 9DVC

• Entry DOI: 10.2210/pdb9dvc/pdb
• EMDB information: 47200
• Descriptor: Soluble cytochrome b562, Cell shape-determining protein MreC, Rod shape-determining protein MreD, ... (5 entities in total)
• Functional Keywords: peptidoglycan synthesis regulator, s-component fold, rod complex, seds activator, membrane protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 7
• Total formula weight: 149515.89

Authors

Gilman, M.S.A.,Kruse, A.C. (deposition date: 2024-10-07, release date: 2025-10-15, Last modification date: 2026-04-29)

Primary citation

Gilman, M.S.A.,Shlosman, I.,Guerra, D.D.S.,Domecillo, M.,Fivenson, E.M.,Bourett, C.,Bernhardt, T.G.,Polizzi, N.F.,Loparo, J.J.,Kruse, A.C.
Conformational regulation of two essential activators of bacterial cell elongation.
Proc.Natl.Acad.Sci.USA, 122:e2514198122-e2514198122, 2025

PubMed Abstract: The peptidoglycan (PG) cell wall is critical for bacterial growth and survival and is a primary antibiotic target. MreD is an essential accessory factor of the Rod complex, which carries out PG synthesis during elongation, yet little is known about how MreD facilitates this process. Here, we present the cryoelectron microscopy structure of MreD in complex with another essential Rod complex component, MreC. The structure reveals that a periplasmic-facing pocket of MreD interacts with multiple membrane-proximal regions of MreC. We use single-molecule FRET to show that MreD controls the conformation of MreC through these contacts, inducing a state primed for Rod complex activation. Using as a model, we demonstrate that disrupting these interactions abolishes Rod complex activity in vivo. Our findings reveal the role of MreD in bacterial cell shape determination and highlight its potential as an antibiotic target.

PubMed: 41183199
DOI: 10.1073/pnas.2514198122

Experimental method

ELECTRON MICROSCOPY (7.4 Å)