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1FFH

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

1FFH の概要
エントリーDOI10.2210/pdb1ffh/pdb
分子名称FFH, MAGNESIUM ION (3 entities in total)
機能のキーワードffh, srp, gtpase, signal recognition particle, ribonucleoprotein
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32280.56
構造登録者
Freymann, D.M.,Keenan, R.J.,Stroud, R.M.,Walter, P. (登録日: 1996-12-30, 公開日: 1997-12-31, 最終更新日: 2024-02-07)
主引用文献Freymann, D.M.,Keenan, R.J.,Stroud, R.M.,Walter, P.
Structure of the conserved GTPase domain of the signal recognition particle.
Nature, 385:361-364, 1997
Cited by
PubMed Abstract: The signal-recognition particle (SRP) and its receptor (SR) function in the co-translational targeting of nascent protein-ribosome complexes to the membrane translocation apparatus. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-alpha subunit (termed FtsY). Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other. The sequence of Ffh suggests three domains: an amino-terminal N domain of unknown function, a central GTPase G domain, and a methionine-rich M domain that binds both SRP RNA and signal peptides. Sequence conservation suggests that structurally similar N and G domains are present in FtsY. Here we report the structure of the nucleotide-free form of the NG fragment of Ffh. Consistent with a role for apo Ffh in protein targeting, the side chains of the empty active-site pocket form a tight network of interactions which may stabilize the nucleotide-free protein. The structural relationship between the two domains suggests that the N domain senses or controls the nucleotide occupancy of the GTPase domain. A structural subdomain unique to these evolutionarily conserved GTPases constitutes them as a distinct subfamily in the GTPase superfamily.
PubMed: 9002524
DOI: 10.1038/385361a0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.05 Å)
構造検証レポート
Validation report summary of 1ffh
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2025-07-02に公開中

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