9QB8

Lymphostatin - Conformation II - pH 8 Hepes

9QB8 の概要

• エントリーDOI: 10.2210/pdb9qb8/pdb
• EMDBエントリー: 52990
• 分子名称: Lymphostatin, MANGANESE (II) ION (2 entities in total)
• 機能のキーワード: virulence factor lymphostatin lifa conformation ii, toxin
• 由来する生物種: Escherichia coli O127:H6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 366476.16

構造登録者

Bottcher, B.,Schneider, R.,Griessmann, M.,Ramussen, T. (登録日: 2025-02-28, 公開日: 2025-07-16, 最終更新日: 2025-07-23)

主引用文献

Griessmann, M.,Rasmussen, T.,Flegler, V.J.,Kraft, C.,Schneider, R.,Hateley, M.,Spantzel, L.,Stevens, M.P.,Borsch, M.,Bottcher, B.
Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli.
Nat Commun, 16:5389-5389, 2025

PubMed Abstract: Lymphostatin is a key virulence factor of enteropathogenic and enterohaemorrhagic Escherichia coli, playing roles in bacterial colonisation of the gut and in the inhibition of lymphocyte proliferation and proinflammatory responses. The protein's glycosyltransferase and cysteine protease motifs are required for activity against lymphocytes, but high-resolution structural information has proven elusive. Here, we describe the structure of lymphostatin from enteropathogenic E. coli O127:H6, determined by electron cryo-microscopy at different pH values. We observe three conformations of a highly complex molecule with two glycosyltransferase domains, one PaToxP-like protease domain, an ADP-ribosyltransferase domain, a vertex domain and a delivery domain. Long linkers hold these domains together and occlude the catalytic sites of the N-terminal glycosyltransferase and protease domains. Lymphostatin binds to bovine T-lymphocytes and HEK-293T cells, forming clusters at the plasma membrane that are internalized. With six distinct domains, lymphostatin can be regarded as a multitool of pathogenic Escherichia coli, enabling complex interactions with host cells.

PubMed: 40562750
DOI: 10.1038/s41467-025-60995-9

実験手法

ELECTRON MICROSCOPY (3.4 Å)