1OTN

Calcium-binding mutant of the Internalin B LRR domain

1OTN の概要

• エントリーDOI: 10.2210/pdb1otn/pdb
• 関連するPDBエントリー: 1OTM 1OTO 1d0b
• 分子名称: Internalin B, CALCIUM ION (3 entities in total)
• 機能のキーワード: internalin, inlb, calcium-binding, invasion, listeria, cell adhesion
• 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: 26213.07

構造登録者

Marino, M.,Copp, J.,Dramsi, S.,Chapman, T.,van der Geer, P.,Cossart, P.,Ghosh, P. (登録日: 2003-03-21, 公開日: 2004-03-30, 最終更新日: 2023-08-16)

主引用文献

Marino, M.,Banerjee, M.,Copp, J.,Dramsi, S.,Chapman, T.,Van Der Geer, P.,Cossart, P.,Ghosh, P.
Characterization of the calcium-binding sites of Listeria monocytogenes InlB
Biochem.Biophys.Res.Commun., 316:379-386, 2004

PubMed Abstract: The Listeria monocytogenes protein InlB promotes invasion of mammalian cells through activation of the receptor tyrosine kinase Met. The InlB N-cap, a approximately 40 residue part of the domain that binds Met, was previously observed to bind two calcium ions in a novel and unusually exposed manner. Because subsequent work raised questions about the existence of these calcium-binding sites, we assayed calcium binding in solution to the InlB N-cap. We show that calcium ions are bound with dissociation constants in the low micromolar range at the two identified sites, and that the sites interact with one another. We demonstrate that the calcium ions are not required for structure, and also find that they have no appreciable effect on Met activation or intracellular invasion. Therefore, our results indicate that the sites are fortuitous in InlB, but also suggest that the simple architecture of the sites may be adaptable for protein engineering purposes.

PubMed: 15020228
DOI: 10.1016/j.bbrc.2004.02.064

実験手法

X-RAY DIFFRACTION (1.97 Å)