Sandbox Reserved 816

From Proteopedia

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This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.

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Introduction

Internalin K is a protein from Listeria monocytogene , which is a Gram-positive bacterium human pathogen. Its ability to survive in the human intestine and to cross a variety of membranes, including mucosal, intestinal, placental, and blood–brain barriers, allows it to generate illnesses ranging from gastroenteritis in healthy individuals to bacteremia and meningitis in immunocompromised patients, as well as mother-to-child infections. Listeria monocytogene can survive in a variety of cell types and proteins of the internalin family have been shown to play a key role in this survival.

The three-dimensional strsuctures of internalin protein have revealed a common N-terminal with leucine-rich repeats (LRRs). Their C-terminal is distinct and implies the specific role of the internalin. Among those proteins, Internalin K, outcome of gene lmo1290 in Listeria monocytogene, is a surface-associated molecule that can interact with major vault protein, a cytoplasmic rubonucleoprotein particle.

Internalin K is a four-domain protein with a “bent arm” morphology. The recognition of major vault protein domain is locatized at the “elbow” region.

spinqualitylabelsall models Internalin K dimer Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

major vault protein

Listeria monocytogene

Image:Chain1.png