1m9s

From Proteopedia

Revision as of 10:40, 20 March 2008

Crystal structure of Internalin B (InlB), a Listeria monocytogenes virulence protein containing SH3-like domains.

Overview

InlB, a surface-localized protein of Listeria monocytogenes, induces phagocytosis in non-phagocytic mammalian cells by activating Met, a receptor tyrosine kinase. InlB also binds glycosaminoglycans and the protein gC1q-R, two additional host ligands implicated in invasion. We present the structure of InlB, revealing a highly elongated molecule with leucine-rich repeats that bind Met at one end, and GW domains that dissociably bind the bacterial surface at the other. Surprisingly, the GW domains are seen to resemble SH3 domains. Despite this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. However, we do show that the GW domains, in addition to binding glycosaminoglycans, bind gC1q-R specifically, and that this binding requires release of InlB from the bacterial surface. Dissociable attachment to the bacterial surface via the GW domains may be responsible for restricting Met activation to a small, localized area of the host cell and for coupling InlB-induced host membrane dynamics with bacterial proximity during invasion.

About this Structure

1M9S is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.

Reference

GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands., Marino M, Banerjee M, Jonquieres R, Cossart P, Ghosh P, EMBO J. 2002 Nov 1;21(21):5623-34. PMID:12411480

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