1O6V

Internalin (INLA, Listeria monocytogenes) - functional domain, uncomplexed

1O6V の概要

• エントリーDOI: 10.2210/pdb1o6v/pdb
• 関連するPDBエントリー: 1O6S 1O6T
• 分子名称: INTERNALIN A, CALCIUM ION (3 entities in total)
• 機能のキーワード: cell adhesion, bacterial infection, extracellular recognition, cell wall attached, leucine rich repeat
• 由来する生物種: LISTERIA MONOCYTOGENES
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 100558.42

構造登録者

Schubert, W.-D.,Urbanke, C.,Ziehm, T.,Beier, V.,Machner, M.P.,Domann, E.,Wehland, J.,Chakraborty, T.,Heinz, D.W. (登録日: 2002-10-16, 公開日: 2002-12-23, 最終更新日: 2024-05-08)

主引用文献

Schubert, W.-D.,Urbanke, C.,Ziehm, T.,Beier, V.,Machner, M.P.,Domann, E.,Wehland, J.,Chakraborty, T.,Heinz, D.W.
Structure of Internalin, a Major Invasion Protein of Listeria Monocytogenes, in Complex with its Human Receptor E-Cadherin
Cell(Cambridge,Mass.), 111:825-, 2002

PubMed Abstract: Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.

PubMed: 12526809
DOI: 10.1016/S0092-8674(02)01136-4

実験手法

X-RAY DIFFRACTION (1.5 Å)