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TitleYidC and Oxa1 form dimeric insertion pores on the translating ribosome.
Journal, issue, pagesMol Cell, Vol. 34, Issue 3, Page 344-353, Year 2009
Publish dateMay 15, 2009
AuthorsRebecca Kohler / Daniel Boehringer / Basil Greber / Rouven Bingel-Erlenmeyer / Ian Collinson / Christiane Schaffitzel / Nenad Ban /
PubMed AbstractThe YidC/Oxa1/Alb3 family of membrane proteins facilitates the insertion and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here we present the structures of both ...The YidC/Oxa1/Alb3 family of membrane proteins facilitates the insertion and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here we present the structures of both Escherichia coli YidC and Saccharomyces cerevisiae Oxa1 bound to E. coli ribosome nascent chain complexes determined by cryo-electron microscopy. Dimers of YidC and Oxa1 are localized above the exit of the ribosomal tunnel. Crosslinking experiments show that the ribosome specifically stabilizes the dimeric state. Functionally important and conserved transmembrane helices of YidC and Oxa1 were localized at the dimer interface by cysteine crosslinking. Both Oxa1 and YidC dimers contact the ribosome at ribosomal protein L23 and conserved rRNA helices 59 and 24, similarly to what was observed for the nonhomologous SecYEG translocon. We suggest that dimers of the YidC and Oxa1 proteins form insertion pores and share a common overall architecture with the SecY monomer.
External linksMol Cell / PubMed:19450532
MethodsEM (single particle)
Resolution14.4 - 18.1 Å
Structure data

EMDB-1615:
Three-dimensional structure of YidC bound to the translating ribosome
Method: EM (single particle) / Resolution: 14.4 Å

EMDB-1616:
Three-dimensional structure of Oxa1 bound to the translating ribosome
Method: EM (single particle) / Resolution: 18.1 Å

Source
  • Escherichia coli (E. coli)
  • Escherichia coli K-12 (bacteria)
  • Saccharomyces cerevisiae (brewer's yeast)

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