5GKM

Crystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone ClpD from Arabidopsis thaliana

5GKM の概要

• エントリーDOI: 10.2210/pdb5gkm/pdb
• 関連するPDBエントリー: 5GUI
• 分子名称: AT5g51070/K3K7_27 (2 entities in total)
• 機能のキーワード: chaperone, protease, clp
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35327.98

構造登録者

Mohapatra, C.,Vasudevan, D. (登録日: 2016-07-04, 公開日: 2017-03-22, 最終更新日: 2023-11-08)

主引用文献

Mohapatra, C.,Kumar Jagdev, M.,Vasudevan, D.
Crystal structures reveal N-terminal Domain of Arabidopsis thaliana ClpD to be highly divergent from that of ClpC1.
Sci Rep, 7:44366-44366, 2017

PubMed Abstract: The caseinolytic protease machinery associated chaperone protein ClpC is known to be present in bacteria, plants and other eukaryotes, whereas ClpD is unique to plants. Plant ClpC and ClpD proteins get localized into chloroplast stroma. Herein, we report high resolution crystal structures of the N-terminal domain of Arabidopsis thaliana ClpC1 and ClpD. Surprisingly, AtClpD, but not AtClpC1, deviates from the typical N-terminal repeat domain organization of known Clp chaperones and have only seven α-helices, instead of eight. In addition, the loop connecting the two halves of AtClpD NTD is longer and covers the region which in case of AtClpC1 is thought to contribute to adaptor protein interaction. Taken together, the N-terminal domain of AtClpD has a divergent structural organization compared to any known Clp chaperones which hints towards its specific role during plant stress conditions, as opposed to that in the maintenance of chloroplastic homeostasis by AtClpC1. Conservation of residues in the NTD that are responsible for the binding of the cyclic peptide activator - Cyclomarin A, as reported for mycobacterial ClpC1 suggests that the peptide could be used as an activator to both AtClpC1 and AtClpD, which could be useful in their detailed in vitro functional characterization.

PubMed: 28287170
DOI: 10.1038/srep44366

実験手法

X-RAY DIFFRACTION (1.6 Å)