9JNS
50S precursor - Erm complex (C-II)
Summary for 9JNS
| Entry DOI | 10.2210/pdb9jns/pdb |
| EMDB information | 61625 |
| Descriptor | 50S ribosomal protein L32, 50S ribosomal protein L17, 50S ribosomal protein L19, ... (18 entities in total) |
| Functional Keywords | 50s precursor, erm, methyltransferase, antibiotic resistance, ribosome-protein complex, ribosome |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 18 |
| Total formula weight | 1172775.44 |
| Authors | Sengupta, S.,Mukherjee, R.,Pilsl, M.,Bagale, S.,Adhikary, A.D.,Borkar, A.,Pradeepkumar, P.I.,Engel, C.,Chowdhury, A.,Kaushal, P.S.,Anand, R. (deposition date: 2024-09-23, release date: 2025-10-29, Last modification date: 2025-12-10) |
| Primary citation | Sengupta, S.,Mukherjee, R.,Pilsl, M.,Bagale, S.,Adhikary, A.D.,Borkar, A.N.,Pradeepkumar, P.I.,Engel, C.,Chowdhury, A.,Kaushal, P.S.,Anand, R. Mechanistic insights into 50 S precursor recognition and targeting by erythromycin resistance methyltransferase. Sci Adv, 11:eaea1545-eaea1545, 2025 Cited by PubMed Abstract: Erythromycin resistance methyltransferases (Erms) confer resistance to macrolide, lincosamide, and streptogramin B antibiotics by methylating an internal base (A2058, numbering) in an elusive precursor ribosomal state. Here, we capture the 50 ribosomal precursor-Erm complex by cryo-EM and show that a transient pocket formed in the early steps of ribosome biogenesis, situated 35 angstrom from the methylation site, serves as an anchor for the auxiliary C-terminal domain of Erm, thereby playing a crucial role in achieving specificity in this short-lived substrate with evolving structural features. Cryo-EM reveals that the catalytic Rossman fold of Erm undergoes a swaying motion to facilitate substrate scouting. Corroboratory smFRET studies show that for effective catalysis, Erm transitions between multiple conformations, an effective strategy adopted to orient the dynamic helix where methylation occurs. Unraveling this unique mechanism of targeting adopted by Erm paves the way for selective design of allosteric inhibitors directed toward reversing MLS resistance. PubMed: 41296849DOI: 10.1126/sciadv.aea1545 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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