1XEU

Crystal Structure of Internalin C from Listeria monocytogenes

1XEU の概要

• エントリーDOI: 10.2210/pdb1xeu/pdb
• 分子名称: internalin C (2 entities in total)
• 機能のキーワード: listeria monocytogenes; cellular invasion; internalin c; leucine-rich repeat; crystal structure, cell invasion
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29567.39

構造登録者

Ooi, A.,Hussain, S.,Seyedarabi, A.,Pickersgill, R.W. (登録日: 2004-09-13, 公開日: 2005-08-30, 最終更新日: 2024-04-03)

主引用文献

Ooi, A.,Hussain, S.,Seyedarabi, A.,Pickersgill, R.W.
Structure of internalin C from Listeria monocytogenes.
Acta Crystallogr.,Sect.D, 62:1287-1293, 2006

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: 17057330
DOI: 10.1107/S0907444906026746

実験手法

X-RAY DIFFRACTION (2.05 Å)