6YPU

Acinetobacter baumannii ribosome-amikacin complex - 30S subunit body

Summary for 6YPU

• Entry DOI: 10.2210/pdb6ypu/pdb
• EMDB information: 10869
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S16, 30S ribosomal protein S17, ... (16 entities in total)
• Functional Keywords: antibiotic, amikacin, translation, ribosome
• Biological source: Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81); More
• Total number of polymer chains: 15
• Total formula weight: 1183150.25

Authors

Nicholson, D.,Edwards, T.A.,O'Neill, A.J.,Ranson, N.A. (deposition date: 2020-04-16, 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

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: 32857965
DOI: 10.1016/j.str.2020.08.004

Experimental method

ELECTRON MICROSCOPY (2.9 Å)