4YJM

The apo structure of Agrobacterium tumefaciens ClpS2

4YJM の概要

• エントリーDOI: 10.2210/pdb4yjm/pdb
• 関連するPDBエントリー: 4YJX 4YKA
• 分子名称: ATP-dependent Clp protease adapter protein ClpS 2 (2 entities in total)
• 機能のキーワード: n-end rule, protease adaptor, protein binding
• 由来する生物種: Agrobacterium tumefaciens (strain C58 / ATCC 33970)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46834.75

構造登録者

Stein, B.,Grant, R.A.,Sauer, R.T.,Baker, T.A. (登録日: 2015-03-03, 公開日: 2016-01-27, 最終更新日: 2023-09-27)

主引用文献

Stein, B.J.,Grant, R.A.,Sauer, R.T.,Baker, T.A.
Structural Basis of an N-Degron Adaptor with More Stringent Specificity.
Structure, 24:232-242, 2016

PubMed Abstract: The N-end rule dictates that a protein's N-terminal residue determines its half-life. In bacteria, the ClpS adaptor mediates N-end-rule degradation, by recognizing proteins bearing specific N-terminal residues and delivering them to the ClpAP AAA+ protease. Unlike most bacterial clades, many α-proteobacteria encode two ClpS paralogs, ClpS1 and ClpS2. Here, we demonstrate that both ClpS1 and ClpS2 from A. tumefaciens deliver N-end-rule substrates to ClpA, but ClpS2 has more stringent binding specificity, recognizing only a subset of the canonical bacterial N-end-rule residues. The basis of this enhanced specificity is addressed by crystal structures of ClpS2, with and without ligand, and structure-guided mutagenesis, revealing protein conformational changes and remodeling in the substrate-binding pocket. We find that ClpS1 and ClpS2 are differentially expressed during growth in A. tumefaciens and conclude that the use of multiple ClpS paralogs allows fine-tuning of N-end-rule degradation at the level of substrate recognition.

PubMed: 26805523
DOI: 10.1016/j.str.2015.12.008

実験手法

X-RAY DIFFRACTION (1.952 Å)