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TitleCryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor.
Journal, issue, pagesNat Struct Mol Biol, Vol. 18, Issue 1, Page 88-90, Year 2011
Publish dateDec 12, 2010
AuthorsLeandro F Estrozi / Daniel Boehringer / Shu-Ou Shan / Nenad Ban / Christiane Schaffitzel /
PubMed AbstractWe report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the ...We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.
External linksNat Struct Mol Biol / PubMed:21151118 / PubMed Central
MethodsEM (single particle)
Resolution13.5 Å
Structure data

1762

2xkv

EMDB-1762: Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor
PDB-2xkv: Atomic Model of the SRP-FtsY Early Conformation
Method: EM (single particle) / Resolution: 13.5 Å

Source
  • escherichia coli (E. coli)
KeywordsPROTEIN TRANSPORT

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