Log in to save to my catalogue

A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translati...

A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translati...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e950afdd22974cc8a096e6e992509d62

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2016-07, Vol.7 (1), p.12026-14, Article 12026

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Nascent polypeptides can induce ribosome stalling, regulating downstream genes. Stalling of ErmBL peptide translation in the presence of the macrolide antibiotic erythromycin leads to resistance in
Streptococcus sanguis
. To reveal this stalling mechanism we obtained 3.6-Å-resolution cryo-EM structures of ErmBL-stalled ribosomes with erythrom...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_e950afdd22974cc8a096e6e992509d62

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e950afdd22974cc8a096e6e992509d62

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms12026

How to access this item