6V39
Cryo-EM structure of the Acinetobacter baumannii Ribosome: 70S with P-site tRNA
This is a non-PDB format compatible entry.
Summary for 6V39
| Entry DOI | 10.2210/pdb6v39/pdb |
| EMDB information | 21030 |
| Descriptor | 50S ribosomal protein L33, 50S ribosomal protein L5, 50S ribosomal protein L6, ... (58 entities in total) |
| Functional Keywords | ribosome, acinetobacter baumannii |
| Biological source | Acinetobacter sp. CIP 51.11 More |
| Total number of polymer chains | 53 |
| Total formula weight | 2163815.39 |
| Authors | |
| Primary citation | Morgan, C.E.,Huang, W.,Rudin, S.D.,Taylor, D.J.,Kirby, J.E.,Bonomo, R.A.,Yu, E.W. Cryo-electron Microscopy Structure of the Acinetobacter baumannii 70S Ribosome and Implications for New Antibiotic Development. Mbio, 11:-, 2020 Cited by PubMed Abstract: Antimicrobial resistance is a major health threat as it limits treatment options for infection. At the forefront of this serious issue is , a Gram-negative opportunistic pathogen that exhibits the remarkable ability to resist antibiotics through multiple mechanisms. As bacterial ribosomes represent a target for multiple distinct classes of existing antimicrobial agents, we here use single-particle cryo-electron microscopy (cryo-EM) to elucidate five different structural states of the ribosome, including the 70S, 50S, and 30S forms. We also determined interparticle motions of the 70S ribosome in different tRNA bound states using three-dimensional (3D) variability analysis. Together, our structural data further our understanding of the ribosome from and other Gram-negative pathogens and will enable structure-based drug discovery to combat antibiotic-resistant bacterial infections. is a severe nosocomial threat largely due to its intrinsic antibiotic resistance and remarkable ability to acquire new resistance determinants. The bacterial ribosome serves as a major target for modern antibiotics and the design of new therapeutics. Here, we present cryo-EM structures of the 70S ribosome, revealing several unique species-specific structural features that may facilitate future drug development to combat this recalcitrant bacterial pathogen. PubMed: 31964740DOI: 10.1128/mBio.03117-19 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.04 Å) |
Structure validation
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