| Title: |
Allosteric activation of cell wall synthesis during bacterial growth |
| Authors: |
Shlosman, Irina; Fivenson, Elayne M.; Gilman, Morgan S. A.; Sisley, Tyler A.; Walker, Suzanne; Bernhardt, Thomas G.; Kruse, Andrew C.; Loparo, Joseph J. |
| Contributors: |
U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases; U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences |
| Source: |
Nature Communications ; volume 14, issue 1 ; ISSN 2041-1723 |
| Publisher Information: |
Springer Science and Business Media LLC |
| Publication Year: |
2023 |
| Description: |
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. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1038/s41467-023-39037-9 |
| Availability: |
https://doi.org/10.1038/s41467-023-39037-9; https://www.nature.com/articles/s41467-023-39037-9.pdf; https://www.nature.com/articles/s41467-023-39037-9 |
| Rights: |
https://creativecommons.org/licenses/by/4.0 ; https://creativecommons.org/licenses/by/4.0 |
| Accession Number: |
edsbas.F64D284B |
| Database: |
BASE |