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Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_uu_104041

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM

About this item

Full title

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM

Publisher

Chichester, UK: John Wiley & Sons, Ltd

Journal title

The EMBO journal, 2008-12, Vol.27 (24), p.3322-3331

Language

English

Formats

Publication information

Publisher

Chichester, UK: John Wiley & Sons, Ltd

More information

Scope and Contents

Contents

The accuracy of ribosomal translation is achieved by an initial selection and a proofreading step, mediated by EF‐Tu, which forms a ternary complex with aminoacyl(aa)‐tRNA. To study the binding modes of different aa‐tRNAs, we compared cryo‐EM maps of the kirromycin‐stalled ribosome bound with ternary complexes containing Phe‐tRNA
Phe
, Trp‐tR...

Alternative Titles

Full title

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_swepub_primary_oai_DiVA_org_uu_104041

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_uu_104041

Other Identifiers

ISSN

0261-4189,1460-2075

E-ISSN

1460-2075

DOI

10.1038/emboj.2008.243

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