8E7F

Crystal structure of the autotransporter Ssp from Serratia marcescens.

8E7F の概要

• エントリーDOI: 10.2210/pdb8e7f/pdb
• 分子名称: Extracellular serine protease, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: autotransporter, subtilase, serratia., toxin, hydrolase
• 由来する生物種: Serratia marcescens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67342.97

構造登録者

Hor, L.,Pilapitiya, A.,Panjikar, S.,Paxman, J.J.,Heras, B. (登録日: 2022-08-23, 公開日: 2023-03-08, 最終更新日: 2023-03-15)

主引用文献

Hor, L.,Pilapitiya, A.,McKenna, J.A.,Panjikar, S.,Anderson, M.A.,Desvaux, M.,Paxman, J.J.,Heras, B.
Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function.
Nat Commun, 14:1163-1163, 2023

PubMed Abstract: Autotransporters (ATs) are a large family of bacterial secreted and outer membrane proteins that encompass a wide range of enzymatic activities frequently associated with pathogenic phenotypes. We present the structural and functional characterisation of a subtilase autotransporter, Ssp, from the opportunistic pathogen Serratia marcescens. Although the structures of subtilases have been well documented, this subtilisin-like protein is associated with a 248 residue β-helix and itself includes three finger-like protrusions around its active site involved in substrate interactions. We further reveal that the activity of the subtilase AT is required for entry into epithelial cells as well as causing cellular toxicity. The Ssp structure not only provides details about the subtilase ATs, but also reveals a common framework and function to more distantly related ATs. As such these findings also represent a significant step forward toward understanding the molecular mechanisms underlying the functional divergence in the large AT superfamily.

PubMed: 36859523
DOI: 10.1038/s41467-023-36719-2

実験手法

X-RAY DIFFRACTION (2 Å)