8G02
YES Complex - E. coli MraY, Protein E PhiX174, E. coli SlyD
Summary for 8G02
| Entry DOI | 10.2210/pdb8g02/pdb |
| EMDB information | 29641 29642 |
| Descriptor | Phospho-N-acetylmuramoyl-pentapeptide-transferase, Lysis protein E, Peptidyl-prolyl cis-trans isomerase (3 entities in total) |
| Functional Keywords | inhibitor, antibiotic, chaperone, membrane, bacteriophage, transferase-isomerase complex, transferase/isomerase |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 6 |
| Total formula weight | 136229.87 |
| Authors | Orta, A.K.,Clemons, W.M.,Li, Y.E. (deposition date: 2023-01-31, release date: 2023-07-26, Last modification date: 2024-06-19) |
| Primary citation | Orta, A.K.,Riera, N.,Li, Y.E.,Tanaka, S.,Yun, H.G.,Klaic, L.,Clemons Jr., W.M. The mechanism of the phage-encoded protein antibiotic from Phi X174. Science, 381:eadg9091-eadg9091, 2023 Cited by PubMed Abstract: The historically important phage ΦX174 kills its host bacteria by encoding a 91-residue protein antibiotic called protein E. Using single-particle electron cryo-microscopy, we demonstrate that protein E bridges two bacterial proteins to form the transmembrane YES complex [MraY, protein E, sensitivity to lysis D (SlyD)]. Protein E inhibits peptidoglycan biosynthesis by obstructing the MraY active site leading to loss of lipid I production. We experimentally validate this result for two different viral species, providing a clear model for bacterial lysis and unifying previous experimental data. Additionally, we characterize the MraY structure-revealing features of this essential enzyme-and the structure of the chaperone SlyD bound to a protein. Our structures provide insights into the mechanism of phage-mediated lysis and for structure-based design of phage therapeutics. PubMed: 37440661DOI: 10.1126/science.adg9091 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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