1O6S

Internalin (Listeria monocytogenes) / E-Cadherin (human) Recognition Complex

Summary for 1O6S

• Entry DOI: 10.2210/pdb1o6s/pdb
• Related: 1O6T 1O6V
• Descriptor: INTERNALIN A, E-CADHERIN, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: bacterial infection, leucine rich repeat, cell adhesion, cell-wall surface protein
• Biological source: LISTERIA MONOCYTOGENES; More
• Total number of polymer chains: 2
• Total formula weight: 61948.66

Authors

Schubert, W.-D.,Urbanke, C.,Ziehm, T.,Beier, V.,Machner, M.P.,Domann, E.,Wehland, J.,Chakraborty, T.,Heinz, D.W. (deposition date: 2002-10-13, release date: 2002-12-13, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)