2J7P

GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY

2J7P の概要

• エントリーDOI: 10.2210/pdb2j7p/pdb
• 関連するPDBエントリー: 1FFH 1JPJ 1JPN 1LS1 1NG1 1O87 1OKK 1RJ9 1RY1 2C03 2C04 2CNW 2FFH 2IYL 2J45 2J46 2NG1 3NG1
• 分子名称: SIGNAL RECOGNITION PARTICLE PROTEIN, CELL DIVISION PROTEIN FTSY, 1,2-ETHANEDIOL, ... (8 entities in total)
• 機能のキーワード: inner membrane, membrane targeting, nucleotide-binding, gmppnp, gdp-pnp, signal recognition particle, rna-binding, gtp-binding, cell division, signal sequence recognition, srp, ffh, ftsy, gtpase, membrane, cell cycle, cell division-complex, signal 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: 4
• 化学式量合計: 130654.83

構造登録者

Freymann, D.M. (登録日: 2006-10-14, 公開日: 2006-12-11, 最終更新日: 2023-12-13)

主引用文献

Gawronski-Salerno, J.,Freymann, D.M.
Structure of the Gmppnp-Stabilized Ng Domain Complex of the Srp Gtpases Ffh and Ftsy.
J.Struct.Biol., 158:122-, 2007

PubMed Abstract: Ffh and FtsY are GTPase components of the signal recognition particle co-translational targeting complex that assemble during the SRP cycle to form a GTP-dependent and pseudo twofold symmetric heterodimer. Previously the SRP GTPase heterodimer has been stabilized and purified for crystallographic studies using both the non-hydrolysable GTP analog GMPPCP and the pseudo-transition state analog GDP:AlF4, revealing in both cases a buried nucleotide pair that bridges and forms a key element of the heterodimer interface. A complex of Ffh and FtsY from Thermus aquaticus formed in the presence of the analog GMPPNP could not be obtained, however. The origin of this failure was previously unclear, and it was thought to have arisen from either instability of the analog, or, alternatively, from differences in its interactions within the tightly conscribed composite active site chamber of the complex. Using insights gained from the previous structure determinations, we have now determined the structure of the SRP GTPase targeting heterodimer stabilized by the non-hydrolysable GTP analog GMPPNP. The structure demonstrates how the different GTP analogs are accommodated within the active site chamber despite slight differences in the geometry of the phosphate chain. It also reveals a K+ coordination site at the highly conserved DARGG loop at the N/G interdomain interface.

PubMed: 17184999
DOI: 10.1016/J.JSB.2006.10.025

実験手法

X-RAY DIFFRACTION (1.97 Å)