1OKK

HOMO-HETERODIMERIC COMPLEX OF THE SRP GTPASES

1OKK の概要

• エントリーDOI: 10.2210/pdb1okk/pdb
• 関連するPDBエントリー: 1FFH 1JPJ 1JPN 1LS1 1NG1 1O87 1RJ9 2FFH 2NG1 3NG1
• 分子名称: SIGNAL RECOGNITION PARTICLE PROTEIN, CELL DIVISION PROTEIN FTSY, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, ... (8 entities in total)
• 機能のキーワード: cell cycle, signal recognition-complex, srp, ffh, ftsy, gtpase, membrane targeting, signal sequence recognition
• 由来する生物種: THERMUS AQUATICUS; 詳細
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein (By similarity): P83749
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67928.88

構造登録者

Focia, P.J.,Freymann, D.M. (登録日: 2003-07-26, 公開日: 2004-01-19, 最終更新日: 2023-12-13)

主引用文献

Focia, P.J.,Shepotinovskaya, I.V.,Seidler, J.A.,Freymann, D.M.
Heterodimeric Gtpase Core of the Srp Targeting Complex
Science, 303:373-, 2004

PubMed Abstract: Two structurally homologous guanosine triphosphatase (GTPase) domains interact directly during signal recognition particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The 2.05 angstrom structure of a complex of the NG GTPase domains of Ffh and FtsY reveals a remarkably symmetric heterodimer sequestering a composite active site that contains two bound nucleotides. The structure explains the coordinate activation of the two GTPases. Conformational changes coupled to formation of their extensive interface may function allosterically to signal formation of the targeting complex to the signal-sequence binding site and the translocon. We propose that the complex represents a molecular "latch" and that its disengagement is regulated by completion of assembly of the GTPase active site.

PubMed: 14726591
DOI: 10.1126/SCIENCE.1090827

実験手法

X-RAY DIFFRACTION (2.05 Å)