Structural highlights
Function
SRP54_THEAQ Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity).[HAMAP-Rule:MF_00306]
Publication Abstract from PubMed
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.
Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor.,Estrozi LF, Boehringer D, Shan SO, Ban N, Schaffitzel C Nat Struct Mol Biol. 2011 Jan;18(1):88-90. Epub 2010 Dec 12. PMID:21151118[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Estrozi LF, Boehringer D, Shan SO, Ban N, Schaffitzel C. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nat Struct Mol Biol. 2011 Jan;18(1):88-90. Epub 2010 Dec 12. PMID:21151118 doi:10.1038/nsmb.1952
