2XXA

The Crystal Structure of the Signal Recognition Particle (SRP) in Complex with its Receptor(SR)

2XXA の概要

• エントリーDOI: 10.2210/pdb2xxa/pdb
• 関連するPDBエントリー: 1DUL 1FTS 1HQ1 2J28 2XKV
• 分子名称: SIGNAL RECOGNITION PARTICLE PROTEIN, SRP RECEPTOR FTSY, 4.5S RNA, ... (6 entities in total)
• 機能のキーワード: protein transport, rna/rna binding protein, hydrolase, gtpase
• 由来する生物種: ESCHERICHIA COLI K-12; 詳細
• 細胞内の位置: Cytoplasm: P0AGD7; Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10121
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 232073.68

構造登録者

Ataide, S.F.,Schmitz, N.,Shen, K.,Ke, A.,Shan, S.,Doudna, J.A.,Ban, N. (登録日: 2010-11-09, 公開日: 2011-03-02, 最終更新日: 2023-12-20)

主引用文献

Ataide, S.F.,Schmitz, N.,Shen, K.,Ke, A.,Shan, S.,Doudna, J.A.,Ban, N.
The Crystal Structure of the Signal Recognition Particle in Complex with its Receptor.
Science, 331:881-, 2011

PubMed Abstract: Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. Here, we present the crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR guanine triphosphatase (GTPase) complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. Combined with previous findings, these results suggest that the SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon.

PubMed: 21330537
DOI: 10.1126/SCIENCE.1196473

実験手法

X-RAY DIFFRACTION (3.94 Å)