1XEU
Crystal Structure of Internalin C from Listeria monocytogenes
Summary for 1XEU
| Entry DOI | 10.2210/pdb1xeu/pdb |
| Descriptor | internalin C (2 entities in total) |
| Functional Keywords | listeria monocytogenes; cellular invasion; internalin c; leucine-rich repeat; crystal structure, cell invasion |
| Biological source | Listeria monocytogenes |
| Total number of polymer chains | 1 |
| Total formula weight | 29567.39 |
| Authors | Ooi, A.,Hussain, S.,Seyedarabi, A.,Pickersgill, R.W. (deposition date: 2004-09-13, release date: 2005-08-30, Last modification date: 2024-04-03) |
| Primary citation | Ooi, A.,Hussain, S.,Seyedarabi, A.,Pickersgill, R.W. Structure of internalin C from Listeria monocytogenes. Acta Crystallogr.,Sect.D, 62:1287-1293, 2006 Cited by PubMed Abstract: 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. PubMed: 17057330DOI: 10.1107/S0907444906026746 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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