1FTS
SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI
1FTS の概要
| エントリーDOI | 10.2210/pdb1fts/pdb |
| 分子名称 | FTSY (1 entity in total) |
| 機能のキーワード | signal recognition particle receptor, gtpase, protein targeting |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Cell inner membrane; Peripheral membrane protein: P10121 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 32182.01 |
| 構造登録者 | Montoya, G.,Svensson, C.,Luirink, J.,Sinning, I. (登録日: 1996-11-20, 公開日: 1998-05-20, 最終更新日: 2024-02-07) |
| 主引用文献 | Montoya, G.,Svensson, C.,Luirink, J.,Sinning, I. Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature, 385:365-368, 1997 Cited by PubMed Abstract: Newly synthesized proteins destined either for secretion or incorporation into membranes are targeted to the membrane translocation machinery by a ubiquitous system consisting of a signal-recognition particle (SRP) and its receptor. Both the SRP receptor and the protein within the SRP that binds the signal sequence contain GTPases. These two proteins, together with the RNA component of the SRP, form a complex and thereby regulate each other's GTPase activity. Here we report the structure of the GTPase-containing portion of FtsY, the functional homologue of the SRP receptor of Escherichia coli, at 2.2 A resolution without bound nucleotide. This so-called NG domain displays similarities to the Ras-related GTPases, as well as features unique to the SRP-type GTPases, such as a separate amino-terminal domain, an insertion within the p21ras (Ras) effector domain, and a wide-open GTP-binding region. The structure explains the low affinity of FtsY for GTP, and suggests rearrangements that may occur on nucleotide binding. It also identifies regions potentially involved in the transmission of signals between domains and in interactions with regulatory proteins. PubMed: 9002525DOI: 10.1038/385365a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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