4L3A

Crystal structure of Internalin K (InlK) from Listeria monocytogenes

4L3A の概要

• エントリーDOI: 10.2210/pdb4l3a/pdb
• 関連するPDBエントリー: 4L3F
• 分子名称: Internalin K, MAGNESIUM ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: leucine rich repeat, immune system evasion, major vault protein, cell invasion
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 129442.44

構造登録者

Neves, D. (登録日: 2013-06-05, 公開日: 2013-08-28, 最終更新日: 2024-02-28)

主引用文献

Neves, D.,Job, V.,Dortet, L.,Cossart, P.,Dessen, A.
Structure of Internalin InlK from the Human Pathogen Listeria monocytogenes.
J.Mol.Biol., 425:4520-4529, 2013

PubMed Abstract: Listeria monocytogenes is a human pathogen that employs a wide variety of virulence factors in order to adhere to, invade, and replicate within target cells. Internalins play key roles in processes ranging from adhesion to receptor recognition and are thus essential for infection. Recently, InlK, a surface-associated internalin, was shown to be involved in Listeria's ability to escape from autophagy by recruitment of the major vault protein (MVP) to the bacterial surface. Here, we report the structure of InlK, which harbors four domains arranged in the shape of a "bent arm". The structure supports a role for the "elbow" of InlK in partner recognition, as well as of two Ig-like pedestals intercalated by hinge regions in the projection of InlK away from the surface of the bacterium. The unusual fold and flexibility of InlK could be essential for MVP binding and concealment from recognition by molecules involved in the autophagic process.

PubMed: 23958637
DOI: 10.1016/j.jmb.2013.08.010

実験手法

X-RAY DIFFRACTION (2.591 Å)