3U2A

Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures

3U2A の概要

• エントリーDOI: 10.2210/pdb3u2a/pdb
• 分子名称: GGDEF family protein (2 entities in total)
• 機能のキーワード: phosphodiesterase, proteolysis, cell-cycle, clpxp, cyclic di-gmp, hydrolase
• 由来する生物種: Caulobacter vibrioides
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13978.76

構造登録者

Rood, K.,Clark, N.E.,Garman, S.C.,Chien, P. (登録日: 2011-10-02, 公開日: 2012-05-30, 最終更新日: 2024-11-06)

主引用文献

Rood, K.L.,Clark, N.E.,Stoddard, P.R.,Garman, S.C.,Chien, P.
Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture.
Structure, 20:1223-1232, 2012

PubMed Abstract: In Caulobacter crescentus, the ClpXP protease degrades several crucial cell-cycle regulators, including the phosphodiesterase PdeA. Degradation of PdeA requires the response regulator CpdR and signals a morphological transition in concert with initiation of DNA replication. Here, we report the structure of a Per-Arnt-Sim (PAS) domain of PdeA and show that it is necessary for CpdR-dependent degradation in vivo and in vitro. CpdR acts as an adaptor, tethering the amino-terminal PAS domain to ClpXP and promoting recognition of the weak carboxyl-terminal degron of PdeA, a combination that ensures processive proteolysis. We identify sites on the PAS domain needed for CpdR recognition and find that one subunit of the PdeA dimer can be delivered to ClpXP by its partner. Finally, we show that improper stabilization of PdeA in vivo alters cellular behavior. These results introduce an adaptor/substrate pair for ClpXP and reveal broad diversity in adaptor-mediated proteolysis.

PubMed: 22682744
DOI: 10.1016/j.str.2012.04.019

実験手法

X-RAY DIFFRACTION (1.7 Å)