7P1H

Structure of the V. vulnificus ExoY-G-actin-profilin complex

7P1H の概要

• エントリーDOI: 10.2210/pdb7p1h/pdb
• EMDBエントリー: 13159
• 分子名称: Maltose/maltodextrin-binding periplasmic protein,RTX-toxin, Actin, cytoplasmic 1, Profilin-1, ... (5 entities in total)
• 機能のキーワード: bacterial toxin, g-actin, profilin, toxin
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 148488.26

構造登録者

Belyy, A.,Merino, F.,Raunser, S. (登録日: 2021-07-01, 公開日: 2021-11-17, 最終更新日: 2021-12-01)

主引用文献

Belyy, A.,Merino, F.,Mechold, U.,Raunser, S.
Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens.
Nat Commun, 12:6628-6628, 2021

PubMed Abstract: Bacterial human pathogens secrete initially inactive nucleotidyl cyclases that become potent enzymes by binding to actin inside eukaryotic host cells. The underlying molecular mechanism of this activation is, however, unclear. Here, we report structures of ExoY from Pseudomonas aeruginosa and Vibrio vulnificus bound to their corresponding activators F-actin and profilin-G-actin. The structures reveal that in contrast to the apo-state, two flexible regions become ordered and interact strongly with actin. The specific stabilization of these regions results in an allosteric stabilization of the nucleotide binding pocket and thereby to an activation of the enzyme. Differences in the sequence and conformation of the actin-binding regions are responsible for the selective binding to either F- or G-actin. Other nucleotidyl cyclase toxins that bind to calmodulin rather than actin undergo a similar disordered-to-ordered transition during activation, suggesting that the allosteric activation-by-stabilization mechanism of ExoY is conserved in these enzymes, albeit the different activator.

PubMed: 34785651
DOI: 10.1038/s41467-021-26889-2

実験手法

ELECTRON MICROSCOPY (3.9 Å)