1d0b
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(New page: 200px<br /><applet load="1d0b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0b, resolution 1.86Å" /> '''INTERNALIN B LEUCINE...)
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Revision as of 10:47, 20 November 2007
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INTERNALIN B LEUCINE RICH REPEAT DOMAIN
Overview
The L. monocytogenes protein lnlB activates phosphoinositide 3-kinase and, induces phagocytosis in several mammalian cell types. The 1.86 A, resolution X-ray crystal structure of the leucine-rich repeat domain of, lnlB that is both necessary and sufficient to induce phagocytosis is, presented here. The structure supports a crucial role for calcium in host, cell invasion by L. monocytogenes and supplies a rationale for its, function. Calciums are bound to the protein in an unusually exposed manner, that suggests that the metals may act as a bridge between lnlB and, mammalian cell surface receptors. The structure also identifies surfaces, on the curved and elongated molecule that may constitute additional, interaction sites in forming a bacterial-mammalian signaling complex.
About this Structure
1D0B is a Single protein structure of sequence from Listeria monocytogenes with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes., Marino M, Braun L, Cossart P, Ghosh P, Mol Cell. 1999 Dec;4(6):1063-72. PMID:10635330
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