A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest

When the antibiotic erythromycin is bound to the ribosomal exit tunnel, ErmBL peptide translation stalls and allows translation of the downstream methyltransferase ErmB. Here the authors combine cryo-EM and molecular dynamics simulations to identify the underlying basis for the inhibition of peptide...

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Autores principales:	Stefan Arenz, Lars V. Bock, Michael Graf, C. Axel Innis, Roland Beckmann, Helmut Grubmüller, Andrea C. Vaiana, Daniel N. Wilson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e950afdd22974cc8a096e6e992509d62
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spelling	oai:doaj.org-article:e950afdd22974cc8a096e6e992509d622021-12-02T17:33:10ZA combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest10.1038/ncomms120262041-1723https://doaj.org/article/e950afdd22974cc8a096e6e992509d622016-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms12026https://doaj.org/toc/2041-1723When the antibiotic erythromycin is bound to the ribosomal exit tunnel, ErmBL peptide translation stalls and allows translation of the downstream methyltransferase ErmB. Here the authors combine cryo-EM and molecular dynamics simulations to identify the underlying basis for the inhibition of peptide bond formation that results in ribosome stalling.Stefan ArenzLars V. BockMichael GrafC. Axel InnisRoland BeckmannHelmut GrubmüllerAndrea C. VaianaDaniel N. WilsonNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Stefan Arenz Lars V. Bock Michael Graf C. Axel Innis Roland Beckmann Helmut Grubmüller Andrea C. Vaiana Daniel N. Wilson A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest
description	When the antibiotic erythromycin is bound to the ribosomal exit tunnel, ErmBL peptide translation stalls and allows translation of the downstream methyltransferase ErmB. Here the authors combine cryo-EM and molecular dynamics simulations to identify the underlying basis for the inhibition of peptide bond formation that results in ribosome stalling.
format	article
author	Stefan Arenz Lars V. Bock Michael Graf C. Axel Innis Roland Beckmann Helmut Grubmüller Andrea C. Vaiana Daniel N. Wilson
author_facet	Stefan Arenz Lars V. Bock Michael Graf C. Axel Innis Roland Beckmann Helmut Grubmüller Andrea C. Vaiana Daniel N. Wilson
author_sort	Stefan Arenz
title	A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest
title_short	A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest
title_full	A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest
title_fullStr	A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest
title_full_unstemmed	A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest
title_sort	combined cryo-em and molecular dynamics approach reveals the mechanism of ermbl-mediated translation arrest
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/e950afdd22974cc8a096e6e992509d62
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A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest

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