scholarly journals Antibiotic resistance ABCF proteins reset the peptidyl transferase centre of the ribosome to counter translational arrest

2018 ◽  
Vol 46 (7) ◽  
pp. 3753-3763 ◽  
Author(s):  
Victoriia Murina ◽  
Marje Kasari ◽  
Vasili Hauryliuk ◽  
Gemma C Atkinson
1997 ◽  
Vol 4 (10) ◽  
pp. 775-778 ◽  
Author(s):  
Elisabetta Viani Puglisi ◽  
Rachel Green ◽  
Harry F. Noller ◽  
Joseph D. Puglisi

Nature ◽  
1995 ◽  
Vol 377 (6547) ◽  
pp. 309-314 ◽  
Author(s):  
Raymond R. Samaha ◽  
Rachel Green ◽  
Harry F. Noller

2018 ◽  
Vol 115 (20) ◽  
pp. 5157-5162 ◽  
Author(s):  
Weixin Su ◽  
Veerendra Kumar ◽  
Yichen Ding ◽  
Rya Ero ◽  
Aida Serra ◽  
...  

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.


1982 ◽  
Vol 7 (11) ◽  
pp. 385-386 ◽  
Author(s):  
R.A. Garrett ◽  
Paul Wooley

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