7F3N

Structure of PopP2 in apo form

7F3N の概要

• エントリーDOI: 10.2210/pdb7f3n/pdb
• 分子名称: Type III effector protein popp2 (2 entities in total)
• 機能のキーワード: yopj, popp2, acetyltransferase, transferase
• 由来する生物種: Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37738.67

構造登録者

Xia, Y.,Zhang, Z.M. (登録日: 2021-06-16, 公開日: 2021-11-17, 最終更新日: 2023-11-29)

主引用文献

Xia, Y.,Zou, R.,Escouboue, M.,Zhong, L.,Zhu, C.,Pouzet, C.,Wu, X.,Wang, Y.,Lv, G.,Zhou, H.,Sun, P.,Ding, K.,Deslandes, L.,Yuan, S.,Zhang, Z.M.
Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase.
Nat Commun, 12:5969-5969, 2021

PubMed Abstract: The Yersinia outer protein J (YopJ) family effectors are widely deployed through the type III secretion system by both plant and animal pathogens. As non-canonical acetyltransferases, the enzymatic activities of YopJ family effectors are allosterically activated by the eukaryote-specific ligand inositol hexaphosphate (InsP6). However, the underpinning molecular mechanism remains undefined. Here we present the crystal structure of apo-PopP2, a YopJ family member secreted by the plant pathogen Ralstonia solanacearum. Structural comparison of apo-PopP2 with the InsP6-bound PopP2 reveals a substantial conformational readjustment centered in the substrate-binding site. Combining biochemical and computational analyses, we further identify a mechanism by which the association of InsP6 with PopP2 induces an α-helix-to-β-strand transition in the catalytic core, resulting in stabilization of the substrate recognition helix in the target protein binding site. Together, our study uncovers the molecular basis governing InsP6-mediated allosteric regulation of YopJ family acetyltransferases and further expands the paradigm of fold-switching proteins.

PubMed: 34645811
DOI: 10.1038/s41467-021-26183-1

実験手法

X-RAY DIFFRACTION (2.35185590332 Å)