5E4X

Crystal structure of cpSRP43 chromodomain 3

5E4X の概要

• エントリーDOI: 10.2210/pdb5e4x/pdb
• 分子名称: Signal recognition particle 43 kDa protein, chloroplastic, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: signal recognition particle, cpsrp43, chromodomain 3, chloroplast, transport protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Plastid, chloroplast stroma : O22265
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5705.56

構造登録者

Horn, A.,Ahmed, Y.L.,Wild, K.,Sinning, I. (登録日: 2015-10-07, 公開日: 2015-12-02, 最終更新日: 2024-01-10)

主引用文献

Horn, A.,Hennig, J.,Ahmed, Y.L.,Stier, G.,Wild, K.,Sattler, M.,Sinning, I.
Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.
Nat Commun, 6:8875-8875, 2015

PubMed Abstract: Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.

PubMed: 26568381
DOI: 10.1038/ncomms9875

実験手法

X-RAY DIFFRACTION (2.75 Å)