5HBN

ClpC N-terminal domain with bound phospho-arginine

5HBN の概要

• エントリーDOI: 10.2210/pdb5hbn/pdb
• 分子名称: Negative regulator of genetic competence ClpC/MecB, SULFATE ION, phospho-arginine, ... (5 entities in total)
• 機能のキーワード: clp protease, degradation tag, protein phosphorylation, phospho-residue binding site, hydrolase
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18193.35

構造登録者

Suskiewicz, M.J.,Clausen, T. (登録日: 2016-01-01, 公開日: 2016-10-12, 最終更新日: 2024-01-10)

主引用文献

Trentini, D.B.,Suskiewicz, M.J.,Heuck, A.,Kurzbauer, R.,Deszcz, L.,Mechtler, K.,Clausen, T.
Arginine phosphorylation marks proteins for degradation by a Clp protease.
Nature, 539:48-53, 2016

PubMed Abstract: Protein turnover is a tightly controlled process that is crucial for the removal of aberrant polypeptides and for cellular signalling. Whereas ubiquitin marks eukaryotic proteins for proteasomal degradation, a general tagging system for the equivalent bacterial Clp proteases is not known. Here we describe the targeting mechanism of the ClpC-ClpP proteolytic complex from Bacillus subtilis. Quantitative affinity proteomics using a ClpP-trapping mutant show that proteins phosphorylated on arginine residues are selectively targeted to ClpC-ClpP. In vitro reconstitution experiments demonstrate that arginine phosphorylation by the McsB kinase is required and sufficient for the degradation of substrate proteins. The docking site for phosphoarginine is located in the amino-terminal domain of the ClpC ATPase, as resolved at high resolution in a co-crystal structure. Together, our data demonstrate that phosphoarginine functions as a bona fide degradation tag for the ClpC-ClpP protease. This system, which is widely distributed across Gram-positive bacteria, is functionally analogous to the eukaryotic ubiquitin-proteasome system.

PubMed: 27749819
DOI: 10.1038/nature20122

実験手法

X-RAY DIFFRACTION (1.602 Å)