3B9Q

The crystal structure of cpFtsY from Arabidopsis thaliana

3B9Q の概要

• エントリーDOI: 10.2210/pdb3b9q/pdb
• 分子名称: Chloroplast SRP receptor homolog, alpha subunit CPFTSY, MALONATE ION (3 entities in total)
• 機能のキーワード: cpftsy, srp receptor, protein translocation, gtp-binding, nucleotide-binding, protein transport
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32704.68

構造登録者

Stengel, K.F.,Wild, K.,Sinning, I. (登録日: 2007-11-06, 公開日: 2007-12-25, 最終更新日: 2023-11-01)

主引用文献

Stengel, K.F.,Holdermann, I.,Wild, K.,Sinning, I.
The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site
Febs Lett., 581:5671-5676, 2007

PubMed Abstract: Two GTPases in the signal recognition particle and its receptor (FtsY) regulate protein targeting to the membrane by formation of a heterodimeric complex. The activation of both GTPases in the complex is essential for protein translocation. We present the crystal structure of chloroplast FtsY (cpFtsY) at 1.75 A resolution. The comparison with FtsY structures in different nucleotide bound states shows structural changes relevant for GTPase activation and provides insights in how cpFtsY is pre-organized for complex formation with cpSRP54. The structure contains an amino-terminal amphipathic helix similar to the membrane targeting sequence of Escherichia coli FtsY. In cpFtsY this motif is extended, which might be responsible for the enhanced attachment of the protein to the thylakoid membrane.

PubMed: 18022392
DOI: 10.1016/j.febslet.2007.11.024

実験手法

X-RAY DIFFRACTION (1.75 Å)