1m9s | pdb_00001m9s

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

spinqualitylabelsall models 1m9s, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m9s is a 1 chain structure with sequence from "bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, TB Related: 1d0b, 1h6t, 1h6u, 1cka, 2abl Gene: inlB ("Bacterium monocytogenes hominis" Nyfeldt 1932) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [INLB_LISMO] Mediates the entry of Listeria monocytogenes into cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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