3E70: Structures and conformations in solution of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus Furiosus

In all organisms, a ribonucleoprotein called the signal recognition particle (SRP) and its receptor (SR) target nascent proteins from the ribosome to the translocon for secretion or membrane insertion. We present the first X-ray structures of an archeal FtsY, the receptor from the hyper-thermophile Pyrococcus furiosus (Pfu), in its free and GDP*magnesium-bound forms. The highly charged N-terminal domain of Pfu-FtsY is distinguished by a long N-terminal helix. The basic charges on the surface of this helix are likely to regulate interactions at the membrane. A peripheral GDP bound near a regulatory motif could indicate a site of interaction between the receptor and ribosomal or SRP RNAs. Small angle X-ray scattering and analytical ultracentrifugation indicate that the crystal structure of Pfu-FtsY correlates well with the average conformation in solution. Based on previous structures of two sub-complexes, we propose a model of the core of archeal and eukaryotic SRP*SR targeting complexes.
PDB ID: 3E70Download
MMDB ID: 68005
PDB Deposition Date: 2008/8/17
Updated in MMDB: 2008/11
Experimental Method:
x-ray diffraction
Resolution: 1.97  Å
Source Organism:
Similar Structures:
Biological Unit for 3E70: monomeric; determined by author and by software (PISA)
Molecular Components in 3E70
Label Count Molecule
Protein (1 molecule)
Signal Recognition Particle Receptor
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB