Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics

The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-Å-resolution crystal structure of bactobolin A bound to 70S ribosome–tRNA complex. The antibiotic binds at a previously unseen site in the 50S subunit and displaces tRNA bound at the P-site. It thus likely has a simil...

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Detalles Bibliográficos
Autores principales: Amunts, Alexey, Fiedorczuk, Karol, Truong, Thao T., Chandler, Josephine, Peter Greenberg, E., Ramakrishnan, V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Brevia
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4332689/
https://www.ncbi.nlm.nih.gov/pubmed/25562208
http://dx.doi.org/10.1016/j.jmb.2014.12.018
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author Amunts, Alexey
Fiedorczuk, Karol
Truong, Thao T.
Chandler, Josephine
Peter Greenberg, E.
Ramakrishnan, V.
author_facet Amunts, Alexey
Fiedorczuk, Karol
Truong, Thao T.
Chandler, Josephine
Peter Greenberg, E.
Ramakrishnan, V.
author_sort Amunts, Alexey
collection PubMed
description The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-Å-resolution crystal structure of bactobolin A bound to 70S ribosome–tRNA complex. The antibiotic binds at a previously unseen site in the 50S subunit and displaces tRNA bound at the P-site. It thus likely has a similar mechanism of action as blasticidin S despite binding to a different site. The structure also rationalizes previously identified resistance mutations.
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spelling pubmed-43326892015-03-03 Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics Amunts, Alexey Fiedorczuk, Karol Truong, Thao T. Chandler, Josephine Peter Greenberg, E. Ramakrishnan, V. J Mol Biol Brevia The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-Å-resolution crystal structure of bactobolin A bound to 70S ribosome–tRNA complex. The antibiotic binds at a previously unseen site in the 50S subunit and displaces tRNA bound at the P-site. It thus likely has a similar mechanism of action as blasticidin S despite binding to a different site. The structure also rationalizes previously identified resistance mutations. Elsevier 2015-02-27 /pmc/articles/PMC4332689/ /pubmed/25562208 http://dx.doi.org/10.1016/j.jmb.2014.12.018 Text en © 2014 The Authors. Published by Elsevier Ltd. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Brevia
Amunts, Alexey
Fiedorczuk, Karol
Truong, Thao T.
Chandler, Josephine
Peter Greenberg, E.
Ramakrishnan, V.
Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics
title Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics
title_full Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics
title_fullStr Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics
title_full_unstemmed Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics
title_short Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics
title_sort bactobolin a binds to a site on the 70s ribosome distinct from previously seen antibiotics
topic Brevia
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4332689/
https://www.ncbi.nlm.nih.gov/pubmed/25562208
http://dx.doi.org/10.1016/j.jmb.2014.12.018
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