5ZLU

Ribosome Structure bound to ABC-F protein.

This is a non-PDB format compatible entry.

Summary for 5ZLU

• Entry DOI: 10.2210/pdb5zlu/pdb
• EMDB information: 6934
• Descriptor: RNA (25-mer), 30S ribosomal protein S3, 30S ribosomal protein S4, ... (58 entities in total)
• Functional Keywords: ribosome, antibiotics, macrolides, abc-f protein, azm
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 57
• Total formula weight: 2280891.92

Authors

Su, W.X.,Kumar, V.,Ero, R.,Andrew, S.W.W.,Jian, S.,Yong-Gui, G. (deposition date: 2018-03-29, release date: 2018-08-01, Last modification date: 2019-12-04)

Primary citation

Su, W.,Kumar, V.,Ding, Y.,Ero, R.,Serra, A.,Lee, B.S.T.,Wong, A.S.W.,Shi, J.,Sze, S.K.,Yang, L.,Gao, Y.G.
Ribosome protection by antibiotic resistance ATP-binding cassette protein.
Proc. Natl. Acad. Sci. U.S.A., 115:5157-5162, 2018

PubMed Abstract: The ribosome is one of the richest targets for antibiotics. Unfortunately, antibiotic resistance is an urgent issue in clinical practice. Several ATP-binding cassette family proteins confer resistance to ribosome-targeting antibiotics through a yet unknown mechanism. Among them, MsrE has been implicated in macrolide resistance. Here, we report the cryo-EM structure of ATP form MsrE bound to the ribosome. Unlike previously characterized ribosomal protection proteins, MsrE is shown to bind to ribosomal exit site. Our structure reveals that the domain linker forms a unique needle-like arrangement with two crossed helices connected by an extended loop projecting into the peptidyl-transferase center and the nascent peptide exit tunnel, where numerous antibiotics bind. In combination with biochemical assays, our structure provides insight into how MsrE binding leads to conformational changes, which results in the release of the drug. This mechanism appears to be universal for the ABC-F type ribosome protection proteins.

PubMed: 29712846
DOI: 10.1073/pnas.1803313115

Experimental method

ELECTRON MICROSCOPY (3.6 Å)