3E70
Structures and conformations in solution of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus Furiosus
3E70 の概要
| エントリーDOI | 10.2210/pdb3e70/pdb |
| 関連するPDBエントリー | 3DLU 3DLV 3DM5 3DM9 3DMD |
| 分子名称 | Signal recognition particle receptor, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| 機能のキーワード | signal recognition particle receptor, ftsy, srp-gtpase, protein-targeting, transport protein |
| 由来する生物種 | Pyrococcus furiosus |
| 細胞内の位置 | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q8U051 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37350.61 |
| 構造登録者 | Egea, P.F.,Tsuruta, H.,Napetschnig, J.,Walter, P.,Stroud, R.M. (登録日: 2008-08-17, 公開日: 2008-11-18, 最終更新日: 2023-08-30) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.97 Å) |
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