Structural highlights
6ytf is a 10 chain structure with sequence from Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | Electron Microscopy, Resolution 3Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
D0CD03_ACIB2 Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.[ARBA:ARBA00024998][HAMAP-Rule:MF_01309]
Publication Abstract from PubMed
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.
Structure of the 70S Ribosome from the Human Pathogen Acinetobacter baumannii in Complex with Clinically Relevant Antibiotics.,Nicholson D, Edwards TA, O'Neill AJ, Ranson NA Structure. 2020 Aug 26. pii: S0969-2126(20)30286-0. doi:, 10.1016/j.str.2020.08.004. PMID:32857965[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nicholson D, Edwards TA, O'Neill AJ, Ranson NA. Structure of the 70S Ribosome from the Human Pathogen Acinetobacter baumannii in Complex with Clinically Relevant Antibiotics. Structure. 2020 Oct 6;28(10):1087-1100.e3. PMID:32857965 doi:10.1016/j.str.2020.08.004
