 |
PDBsum entry 3dmd
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
3dmd
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structures of the signal recognition particle receptor from the archaeon pyrococcus furiosus: implications for the targeting step at the membrane.
|
 |
|
Authors
|
 |
P.F.Egea,
H.Tsuruta,
G.P.De leon,
J.Napetschnig,
P.Walter,
R.M.Stroud.
|
 |
|
Ref.
|
 |
Plos One, 2008,
3,
e3619.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |