1xeu
From Proteopedia
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Crystal Structure of Internalin C from Listeria monocytogenes
Overview
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.
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
Page seeded by OCA on Thu Feb 21 15:54:01 2008
