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|Title:||Ribosome protection by antibiotic resistance ATP-binding cassette protein||Authors:||Su, Weixin
Lee, Benjamin Sian Teck
Wong, Andrew See Weng
Sze, Siu Kwan
|Keywords:||Science::Biological sciences||Issue Date:||2018||Source:||Su, W., Kumar, V., Ding, Y., Ero, R., Serra, A., Lee, B. S. T., . . ., Gao, Y.-G. (2018). Ribosome protection by antibiotic resistance ATP-binding cassette protein. Proceedings of the National Academy of Sciences of the United States of America, 115(20), 5157-5162. doi:10.1073/pnas.1803313115||Journal:||Proceedings of the National Academy of Sciences of the United States of America||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.||URI:||https://hdl.handle.net/10356/137714||ISSN:||0027-8424||DOI:||10.1073/pnas.1803313115||Rights:||© 2018 The Author(s) (Published by National Academy of Sciences). All rights reserved.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||SBS Journal Articles|
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