Structural highlights
3kl4 is a 2 chain structure with sequence from Atcc 18824 and Sacs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 2ffh, 1qzx, 1qzw, 1dul, 1j8m, 2j28 |
| Gene: | srp54, SSO0971 (SACS2) |
| Activity: | Signal-recognition-particle GTPase, with EC number 3.6.5.4 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SRP54_SULSO] 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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Targeting of proteins to appropriate subcellular compartments is a crucial process in all living cells. Secretory and membrane proteins usually contain an amino-terminal signal peptide, which is recognized by the signal recognition particle (SRP) when nascent polypeptide chains emerge from the ribosome. The SRP-ribosome nascent chain complex is then targeted through its GTP-dependent interaction with SRP receptor to the protein-conducting channel on endoplasmic reticulum membrane in eukaryotes or plasma membrane in bacteria. A universally conserved component of SRP (refs 1, 2), SRP54 or its bacterial homologue, fifty-four homologue (Ffh), binds the signal peptides, which have a highly divergent sequence divisible into a positively charged n-region, an h-region commonly containing 8-20 hydrophobic residues and a polar c-region. No structure has been reported that exemplifies SRP54 binding of any signal sequence. Here we have produced a fusion protein between Sulfolobus solfataricus SRP54 (Ffh) and a signal peptide connected via a flexible linker. This fusion protein oligomerizes in solution through interaction between the SRP54 and signal peptide moieties belonging to different chains, and it is functional, as demonstrated by its ability to bind SRP RNA and SRP receptor FtsY. We present the crystal structure at 3.5 A resolution of an SRP54-signal peptide complex in the dimer, which reveals how a signal sequence is recognized by SRP54.
Recognition of a signal peptide by the signal recognition particle.,Janda CY, Li J, Oubridge C, Hernandez H, Robinson CV, Nagai K Nature. 2010 May 27;465(7297):507-10. Epub 2010 Apr 4. PMID:20364120[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Janda CY, Li J, Oubridge C, Hernandez H, Robinson CV, Nagai K. Recognition of a signal peptide by the signal recognition particle. Nature. 2010 May 27;465(7297):507-10. Epub 2010 Apr 4. PMID:20364120 doi:10.1038/nature08870
