AI Article Synopsis
- The peptidoglycan cell wall is crucial for bacterial protection and shape, making it a prime target for antibiotics.
- Researchers used advanced techniques to study the essential enzyme RodA-PBP2, revealing that it switches between closed and open states to regulate peptidoglycan synthesis.
- The findings suggest that this opening mechanism could be a common way to control peptidoglycan production during various cellular activities, including cell division.
Article Abstract
The peptidoglycan (PG) cell wall protects bacteria against osmotic lysis and determines cell shape, making this structure a key antibiotic target. Peptidoglycan is a polymer of glycan chains connected by peptide crosslinks, and its synthesis requires precise spatiotemporal coordination between glycan polymerization and crosslinking. However, the molecular mechanism by which these reactions are initiated and coupled is unclear. Here we use single-molecule FRET and cryo-EM to show that an essential PG synthase (RodA-PBP2) responsible for bacterial elongation undergoes dynamic exchange between closed and open states. Structural opening couples the activation of polymerization and crosslinking and is essential in vivo. Given the high conservation of this family of synthases, the opening motion that we uncovered likely represents a conserved regulatory mechanism that controls the activation of PG synthesis during other cellular processes, including cell division.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10257715 | PMC |
| http://dx.doi.org/10.1038/s41467-023-39037-9 | DOI Listing |
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