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1NG1

N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS

1NG1 の概要
エントリーDOI10.2210/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
Freymann, D.M.,Stroud, R.M.,Walter, P. (登録日: 1998-04-30, 公開日: 1999-07-30, 最終更新日: 2024-05-22)
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: 10426959
DOI: 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)
構造検証レポート
Validation report summary of 1ng1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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