4U67
Crystal structure of the large ribosomal subunit (50S) of Deinococcus radiodurans containing a three residue insertion in L22
Summary for 4U67
| Entry DOI | 10.2210/pdb4u67/pdb |
| Descriptor | 50S ribosomal protein L2, 50S ribosomal protein L17, 50S ribosomal protein L18, ... (29 entities in total) |
| Functional Keywords | ribosome, antibiotics, resistance, erythromycin |
| Biological source | Deinococcus radiodurans More |
| Total number of polymer chains | 28 |
| Total formula weight | 1346688.89 |
| Authors | Wekselman, I.,Zimmerman, E.,Rozenberg, H.,Bashan, A.,Yonath, A. (deposition date: 2014-07-28, release date: 2015-08-05, Last modification date: 2024-11-20) |
| Primary citation | Wekselman, I.,Zimmerman, E.,Davidovich, C.,Belousoff, M.,Matzov, D.,Krupkin, M.,Rozenberg, H.,Bashan, A.,Friedlander, G.,Kjeldgaard, J.,Ingmer, H.,Lindahl, L.,Zengel, J.M.,Yonath, A. The Ribosomal Protein uL22 Modulates the Shape of the Protein Exit Tunnel. Structure, 25:1233-1241.e3, 2017 Cited by PubMed Abstract: Erythromycin is a clinically useful antibiotic that binds to an rRNA pocket in the ribosomal exit tunnel. Commonly, resistance to erythromycin is acquired by alterations of rRNA nucleotides that interact with the drug. Mutations in the β hairpin of ribosomal protein uL22, which is rather distal to the erythromycin binding site, also generate resistance to the antibiotic. We have determined the crystal structure of the large ribosomal subunit from Deinococcus radiodurans with a three amino acid insertion within the β hairpin of uL22 that renders resistance to erythromycin. The structure reveals a shift of the β hairpin of the mutated uL22 toward the interior of the exit tunnel, triggering a cascade of structural alterations of rRNA nucleotides that propagate to the erythromycin binding pocket. Our findings support recent studies showing that the interactions between uL22 and specific sequences within nascent chains trigger conformational rearrangements in the exit tunnel. PubMed: 28689968DOI: 10.1016/j.str.2017.06.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.65 Å) |
Structure validation
Download full validation report
