Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/137714
Title: Ribosome protection by antibiotic resistance ATP-binding cassette protein
Authors: Su, Weixin
Kumar, Veerendra
Ding, Yichen
Ero, Rya
Serra, Aida
Lee, Benjamin Sian Teck
Wong, Andrew See Weng
Shi, Jian
Sze, Siu Kwan
Yang, Liang
Gao, Yong-Gui
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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