4Y0C

The structure of Arabidopsis ClpT2

4Y0C の概要

• エントリーDOI: 10.2210/pdb4y0c/pdb
• 関連するPDBエントリー: 4Y0B
• 分子名称: Clp protease-related protein At4g12060, chloroplastic, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: caseinolytic protease, n-domain, alpha helical bundle, plastid, protein binding
• 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: 40071.28

構造登録者

Kimber, M.S.,Schultz, L. (登録日: 2015-02-05, 公開日: 2015-05-13, 最終更新日: 2024-10-30)

主引用文献

Kim, J.,Kimber, M.S.,Nishimura, K.,Friso, G.,Schultz, L.,Ponnala, L.,van Wijk, K.J.
Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts.
Plant Cell, 27:1477-1496, 2015

PubMed Abstract: Plastid ClpT1 and ClpT2 are plant-specific proteins that associate with the ClpPR protease. However, their physiological significance and structures are not understood. Arabidopsis thaliana loss-of-function single clpt1 and clpt2 mutants showed no visible phenotypes, whereas clpt1 clpt2 double mutants showed delayed development, reduced plant growth, and virescent, serrated leaves but were viable and produced seed. The clpt1 and clpt1 clpt2 mutants showed partial destabilization of the ClpPR complex, whereas clpt2 null mutants showed only marginal destabilization. Comparative proteomics of clpt1 clpt2 plants showed a proteostasis phenotype similar to viable mutants in ClpPR core subunits, indicating reduced Clp protease capacity. In vivo and in vitro assays showed that ClpT1 and ClpT2 can independently interact with the single ClpP ring and ClpPR core, but not with the single ClpR ring. We determined ClpT1 and ClpT2 structures (2.4- and 2.0-Å resolution) and detailed the similarities to the N-domains of bacterial ClpA/C chaperones. The ClpT structures suggested a conserved MYFF motif for interaction with the ClpPR core near the interface between the P- and R-rings. In vivo complementation showed that ClpT function and ClpPR core stabilization require the MYFF motif. Several models are presented that may explain how ClpT1,2 contribute to ClpPR protease activity.

PubMed: 25921872
DOI: 10.1105/tpc.15.00106

実験手法

X-RAY DIFFRACTION (1.992 Å)