8TLU
E. coli MraY mutant-T23P
Summary for 8TLU
| Entry DOI | 10.2210/pdb8tlu/pdb |
| EMDB information | 41373 |
| Descriptor | Phospho-N-acetylmuramoyl-pentapeptide-transferase (1 entity in total) |
| Functional Keywords | peptidoglycan, phosphotransferase, membrane protein |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 79811.10 |
| Authors | |
| Primary citation | Marmont, L.S.,Orta, A.K.,Baileeves, B.W.A.,Sychantha, D.,Fernandez-Galliano, A.,Li, Y.E.,Greene, N.G.,Corey, R.A.,Stansfeld, P.J.,Clemons Jr., W.M.,Bernhardt, T.G. Synthesis of lipid-linked precursors of the bacterial cell wall is governed by a feedback control mechanism in Pseudomonas aeruginosa. Nat Microbiol, 9:763-775, 2024 Cited by PubMed Abstract: Many bacterial surface glycans such as the peptidoglycan (PG) cell wall are built from monomeric units linked to a polyprenyl lipid carrier. How this limiting carrier is distributed among competing pathways has remained unclear. Here we describe the isolation of hyperactive variants of Pseudomonas aeruginosa MraY, the enzyme that forms the first lipid-linked PG precursor. These variants result in the elevated production of the final PG precursor lipid II in cells and are hyperactive in vitro. The activated MraY variants have substitutions that map to a cavity on the extracellular side of the dimer interface, far from the active site. Our structural and molecular dynamics results suggest that this cavity is a binding site for externalized lipid II. Overall, our results support a model in which excess externalized lipid II allosterically inhibits MraY, providing a feedback mechanism that prevents the sequestration of lipid carrier in the PG biogenesis pathway. PubMed: 38336881DOI: 10.1038/s41564-024-01603-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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