3DMD

Structures and Conformations in Solution of the Signal Recognition Particle Receptor from the archaeon Pyrococcus furiosus

Summary for 3DMD

• Entry DOI: 10.2210/pdb3dmd/pdb
• Related: 3DM9
• Descriptor: Signal recognition particle receptor, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: signal recognition particle receptor, ftsy, srp-gtpase, protein-targeting, transport protein
• Biological source: Pyrococcus furiosus
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q8U051
• Total number of polymer chains: 3
• Total formula weight: 110832.91

Authors

Egea, P.F.,Tsuruta, H.,Napetschnig, J.,Walter, P.,Stroud, R.M. (deposition date: 2008-06-30, release date: 2008-11-11, Last modification date: 2023-08-30)

Primary citation

Egea, P.F.,Tsuruta, H.,de Leon, G.P.,Napetschnig, J.,Walter, P.,Stroud, R.M.
Structures of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus furiosus: Implications for the Targeting Step at the Membrane.
Plos One, 3:e3619-e3619, 2008

PubMed Abstract: 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.

PubMed: 18978942
DOI: 10.1371/journal.pone.0003619

Experimental method

X-RAY DIFFRACTION (2.21 Å)