PDBsum entry 3dm9

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protein ligands links
Transport protein PDB id
Protein chain
305 a.a. *
PO4 ×4
Waters ×137
* Residue conservation analysis
PDB id:
Name: Transport protein
Title: Structures and conformations in solution of the signal recognition particle receptor from the archaeon pyrococcus furiosus
Structure: Signal recognition particle receptor. Chain: b. Synonym: dpa. Engineered: yes
Source: Pyrococcus furiosus. Organism_taxid: 2261. Strain: dsm3638. Gene: pf1766. Expressed in: escherichia coli.
2.20Å     R-factor:   0.206     R-free:   0.239
Authors: P.F.Egea,H.Tsuruta,J.Napetschnig,P.Walter,R.M.Stroud
Key ref: P.F.Egea et al. (2008). Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane. PLoS One, 3, e3619. PubMed id: 18978942
30-Jun-08     Release date:   11-Nov-08    
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Protein chain
Pfam   ArchSchema ?
Q8U051  (Q8U051_PYRFU) -  Signal recognition particle receptor FtsY
322 a.a.
305 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   4 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     nucleotide binding     3 terms  


PLoS One 3:e3619 (2008)
PubMed id: 18978942  
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.
P.F.Egea, H.Tsuruta, Leon, J.Napetschnig, P.Walter, R.M.Stroud.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20487556 H.Hartman, and T.F.Smith (2010).
GTPases and the origin of the ribosome.
  Biol Direct, 5, 36.  
20855604 P.F.Egea, and R.M.Stroud (2010).
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes.
  Proc Natl Acad Sci U S A, 107, 17182-17187.
PDB code: 3mp7
19912622 M.Mircheva, D.Boy, B.Weiche, F.Hucke, P.Graumann, and H.G.Koch (2009).
Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.
  BMC Biol, 7, 76.  
19293157 N.J.Marty, D.Rajalingam, A.D.Kight, N.E.Lewis, D.Fologea, T.K.Kumar, R.L.Henry, and R.L.Goforth (2009).
The Membrane-binding Motif of the Chloroplast Signal Recognition Particle Receptor (cpFtsY) Regulates GTPase Activity.
  J Biol Chem, 284, 14891-14903.  
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