uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
The structure of the ribosome with elongation factor G trapped in the posttranslocational state
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
Show others and affiliations
2009 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 326, no 5953, 694-699 p.Article in journal (Refereed) Published
Abstract [en]

Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms. The interaction of EF-G with ribosomal elements implicated in stimulating catalysis, such as the L10-L12 stalk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P site) and with mRNA shed light on the role of these elements in EF-G function. The stabilization of the mobile stalks of the ribosome also results in a more complete description of its structure.

Place, publisher, year, edition, pages
2009. Vol. 326, no 5953, 694-699 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-141781DOI: 10.1126/science.1179709PubMedID: 19833919OAI: oai:DiVA.org:uu-141781DiVA: diva2:386223
Available from: 2011-01-12 Created: 2011-01-12 Last updated: 2015-10-02

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

Selmer, Maria

Search in DiVA

By author/editor
Selmer, Maria
By organisation
Structural Molecular Biology
In the same journal
Science
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 390 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf