6TPL

D0-D1 domain of Intimin

6TPL の概要

• エントリーDOI: 10.2210/pdb6tpl/pdb
• 分子名称: Intimin, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: intimin, adhesion, passenger domain, bacterial ig domain, ig, big domain, cell adhesion
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41199.23

構造登録者

Weikum, J.,Leo, J.C.,Morth, J.P. (登録日: 2019-12-13, 公開日: 2021-01-13, 最終更新日: 2024-01-24)

主引用文献

Weikum, J.,Kulakova, A.,Tesei, G.,Yoshimoto, S.,Jaegerum, L.V.,Schutz, M.,Hori, K.,Skepo, M.,Harris, P.,Leo, J.C.,Morth, J.P.
The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action.
Sci Rep, 10:21249-21249, 2020

PubMed Abstract: Enterohemorrhagic and enteropathogenic Escherichia coli are among the most important food-borne pathogens, posing a global health threat. The virulence factor intimin is essential for the attachment of pathogenic E. coli to the intestinal host cell. Intimin consists of four extracellular bacterial immunoglobulin-like (Big) domains, D00-D2, extending into the fifth lectin subdomain (D3) that binds to the Tir-receptor on the host cell. Here, we present the crystal structures of the elusive D00-D0 domains at 1.5 Å and D0-D1 at 1.8 Å resolution, which confirms that the passenger of intimin has five distinct domains. We describe that D00-D0 exhibits a higher degree of rigidity and D00 likely functions as a juncture domain at the outer membrane-extracellular medium interface. We conclude that D00 is a unique Big domain with a specific topology likely found in a broad range of other inverse autotransporters. The accumulated data allows us to model the complete passenger of intimin and propose functionality to the Big domains, D00-D0-D1, extending directly from the membrane.

PubMed: 33277518
DOI: 10.1038/s41598-020-77706-7

実験手法

X-RAY DIFFRACTION (1.8 Å)