3PIP
Crystal structure of the synergistic antibiotic pair lankamycin and lankacidin in complex with the large ribosomal subunit
Summary for 3PIP
| Entry DOI | 10.2210/pdb3pip/pdb |
| Related | 1NKW 1SM1 1YI2 2ZJR 3JQ4 3PIO |
| Descriptor | RIBOSOMAL 23S RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (35 entities in total) |
| Functional Keywords | ribosome, large ribosomal subunit, 50s, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, lankamycin, lankacidin, macrolide, ribosome-antibiotic complex, ribosome/antibiotic |
| Biological source | Deinococcus radiodurans R1 More |
| Total number of polymer chains | 30 |
| Total formula weight | 1367643.59 |
| Authors | Belousoff, M.J.,Shapira, T.,Bashan, A.,Zimmerman, E.,Kinashi, H.,Rozenberg, H.,Yonath, A. (deposition date: 2010-11-07, release date: 2011-02-23, Last modification date: 2024-10-09) |
| Primary citation | Belousoff, M.J.,Shapira, T.,Bashan, A.,Zimmerman, E.,Rozenberg, H.,Arakawa, K.,Kinashi, H.,Yonath, A. Crystal structure of the synergistic antibiotic pair, lankamycin and lankacidin, in complex with the large ribosomal subunit. Proc.Natl.Acad.Sci.USA, 108:2717-2722, 2011 Cited by PubMed Abstract: The structures of the large ribosomal subunit of Deinococcus radiodurans (D50S) in complex with the antibiotic lankamycin (3.2 Å) and a double antibiotic complex of lankamycin and lankacidin C (3.45 Å) have been determined, in continuation of previous crystallographic studies on lankacidin-D50S complex. These two drugs have been previously reported to inhibit ribosomal function with mild synergistic effect. Lankamycin, a member of the macrolide family, binds in a similar manner to erythromycin. However, when in complex with lankacidin, lankamycin is located so that it can form interactions with lankacidin in the adjacent ribosomal binding site. When compared to the well-documented synergistic antibiotics, Streptogramins A and B, the pair of lankacidin and lankamycin bind in similar sites, the peptidyl transferase center and nascent peptide exit tunnel, respectively. Herein, we discuss the structural basis for antibiotic synergism and highlight the key factors involved in ribosomal inhibition. PubMed: 21282615DOI: 10.1073/pnas.1019406108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.45 Å) |
Structure validation
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