1QZW

Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication

1QZW の概要

• エントリーDOI: 10.2210/pdb1qzw/pdb
• 関連するPDBエントリー: 1HQ1 1J8M 1QZX
• 分子名称: 7S RNA, Signal recognition 54 kDa protein (2 entities in total)
• 機能のキーワード: signal recognition particle, srp, ribonucleoprotein complex, protein-rna complex, protein targeting, signaling protein-rna complex, signaling protein/rna
• 由来する生物種: Sulfolobus solfataricus; 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q97ZE7
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 260074.40

構造登録者

Rosendal, K.R.,Wild, K.,Montoya, G.,Sinning, I. (登録日: 2003-09-18, 公開日: 2003-11-18, 最終更新日: 2023-08-23)

主引用文献

Rosendal, K.R.,Wild, K.,Montoya, G.,Sinning, I.
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
Proc.Natl.Acad.Sci.USA, 100:14701-14706, 2003

PubMed Abstract: Targeting of secretory and membrane proteins by the signal recognition particle (SRP) is evolutionarily conserved, and the multidomain protein SRP54 acts as the key player in SRP-mediated protein transport. Binding of a signal peptide to SRP54 at the ribosome is coordinated with GTP binding and subsequent complex formation with the SRP receptor. Because these functions are localized to distinct domains of SRP54, communication between them is essential. We report the crystal structures of SRP54 from the Archaeon Sulfolobus solfataricus with and without its cognate SRP RNA binding site (helix 8) at 4-A resolution. The two structures show the flexibility of the SRP core and the position of SRP54 relative to the RNA. A long linker helix connects the GTPase (G domain) with the signal peptide binding (M) domain, and a hydrophobic contact between the N and M domains relates the signal peptide binding site to the G domain. Hinge regions are identified in the linker between the G and M domains (292-LGMGD) and in the N-terminal part of the M domain, which allow for structural rearrangements within SRP54 upon signal peptide binding at the ribosome.

PubMed: 14657338
DOI: 10.1073/pnas.2436132100

実験手法

X-RAY DIFFRACTION (4.1 Å)