3E70
Structures and conformations in solution of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus Furiosus
Summary for 3E70
Entry DOI | 10.2210/pdb3e70/pdb |
Related | 3DLU 3DLV 3DM5 3DM9 3DMD |
Descriptor | Signal recognition particle receptor, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (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 | 1 |
Total formula weight | 37350.61 |
Authors | Egea, P.F.,Tsuruta, H.,Napetschnig, J.,Walter, P.,Stroud, R.M. (deposition date: 2008-08-17, release date: 2008-11-18, 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 Cited by 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: 18978942DOI: 10.1371/journal.pone.0003619 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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