6YSI
Acinetobacter baumannii ribosome-tigecycline complex - 50S subunit
Summary for 6YSI
| Entry DOI | 10.2210/pdb6ysi/pdb |
| EMDB information | 10898 |
| Descriptor | 50S ribosomal protein L2, 50S ribosomal protein L17, 50S ribosomal protein L18, ... (34 entities in total) |
| Functional Keywords | antibiotic, tigecycline, translation, ribosome |
| Biological source | Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 More |
| Total number of polymer chains | 32 |
| Total formula weight | 1387934.74 |
| Authors | Nicholson, D.,Edwards, T.A.,O'Neill, A.J.,Ranson, N.A. (deposition date: 2020-04-22, release date: 2020-09-16, Last modification date: 2024-05-22) |
| Primary citation | Nicholson, D.,Edwards, T.A.,O'Neill, A.J.,Ranson, N.A. Structure of the 70S Ribosome from the Human Pathogen Acinetobacter baumannii in Complex with Clinically Relevant Antibiotics. Structure, 28:1087-1100.e3, 2020 Cited by PubMed Abstract: Acinetobacter baumannii is a Gram-negative bacterium primarily associated with hospital-acquired, often multidrug-resistant (MDR) infections. The ribosome-targeting antibiotics amikacin and tigecycline are among the limited arsenal of drugs available for treatment of such infections. We present high-resolution structures of the 70S ribosome from A. baumannii in complex with these antibiotics, as determined by cryoelectron microscopy. Comparison with the ribosomes of other bacteria reveals several unique structural features at functionally important sites, including around the exit of the polypeptide tunnel and the periphery of the subunit interface. The structures also reveal the mode and site of interaction of these drugs with the ribosome. This work paves the way for the design of new inhibitors of translation to address infections caused by MDR A. baumannii. PubMed: 32857965DOI: 10.1016/j.str.2020.08.004 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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