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1xeu

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{{STRUCTURE_1xeu| PDB=1xeu | SCENE= }}
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'''Crystal Structure of Internalin C from Listeria monocytogenes'''
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===Crystal Structure of Internalin C from Listeria monocytogenes===
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==Overview==
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The crystal structure of internalin C (InlC) from Listeria monocytogenes has been determined at 2.0 A resolution. Several observations implicate InlC in infection: inlC has the same transcriptional activator as other virulence genes, it is only present in pathogenic Listeria strains and an inlC deletion mutant is significantly less virulent. While the extended concave receptor-binding surfaces of the leucine-rich repeat (LRR) domains of internalins A and B have aromatic clusters involved in receptor binding, the corresponding surface of InlC is smaller, flatter and more hydrophilic, suggesting that InlC may be involved in weak or transient associations with receptors; this may help explain why no receptor has yet been discovered for InlC. In contrast, the Ig-like domain, to which the LRR domain is fused, has surface aromatics that may be of functional importance, possibly being involved in binding to the surface of the bacteria or in receptor binding.
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==About this Structure==
==About this Structure==
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[[Category: Leucine-rich repeat]]
[[Category: Leucine-rich repeat]]
[[Category: Listeria monocytogene]]
[[Category: Listeria monocytogene]]
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Revision as of 12:32, 28 July 2008

Image:1xeu.png

Template:STRUCTURE 1xeu

Crystal Structure of Internalin C from Listeria monocytogenes

Template:ABSTRACT PUBMED 17057330

About this Structure

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

Reference

Structure of internalin C from Listeria monocytogenes., Ooi A, Hussain S, Seyedarabi A, Pickersgill RW, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1287-93. Epub 2006, Oct 18. PMID:17057330

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