1m9s

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(New page: 200px<br /><applet load="1m9s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m9s, resolution 2.65&Aring;" /> '''Crystal structure of...)
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[[Image:1m9s.jpg|left|200px]]<br /><applet load="1m9s" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m9s, resolution 2.65&Aring;" />
caption="1m9s, resolution 2.65&Aring;" />
'''Crystal structure of Internalin B (InlB), a Listeria monocytogenes virulence protein containing SH3-like domains.'''<br />
'''Crystal structure of Internalin B (InlB), a Listeria monocytogenes virulence protein containing SH3-like domains.'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1M9S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with TB and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M9S OCA].
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1M9S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with <scene name='pdbligand=TB:'>TB</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9S OCA].
==Reference==
==Reference==
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[[Category: sh3 domains]]
[[Category: sh3 domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:15:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:00 2008''

Revision as of 11:53, 21 February 2008

Image:1m9s.jpg

1m9s, resolution 2.65Å

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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 with and as ligands. 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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