1NG1
N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
1NG1 の概要
エントリーDOI | 10.2210/pdb1ng1/pdb |
分子名称 | SIGNAL SEQUENCE RECOGNITION PROTEIN FFH, CADMIUM ION, MAGNESIUM ION, ... (7 entities in total) |
機能のキーワード | ffh, srp, gtpase, signal recognition particle, gdp, mg, signal recognition |
由来する生物種 | Thermus aquaticus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 33555.83 |
構造登録者 | |
主引用文献 | Freymann, D.M.,Keenan, R.J.,Stroud, R.M.,Walter, P. Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat.Struct.Biol., 6:793-801, 1999 Cited by PubMed Abstract: Ffh is a component of a bacterial ribonucleoprotein complex homologous to the signal recognition particle (SRP) of eukaryotes. It comprises three domains that mediate both binding to the hydrophobic signal sequence of the nascent polypeptide and the GTP-dependent interaction of Ffh with a structurally homologous GTPase of the SRP receptor. The X-ray structures of the two-domain 'NG' GTPase of Ffh in complex with Mg2+GDP and GDP have been determined at 2.0 A resolution. The structures explain the low nucleotide affinity of Ffh and locate two regions of structural mobility at opposite sides of the nucleotide-binding site. One of these regions includes highly conserved sequence motifs that presumably contribute to the structural trigger signaling the GTP-bound state. The other includes the highly conserved interface between the N and G domains, and supports the hypothesis that the N domain regulates or signals the nucleotide occupancy of the G domain. PubMed: 10426959DOI: 10.1038/11572 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.03 Å) |
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