In vitro assembly of Haemophilus influenzae adhesin transmembrane domain and studies on the electrostatic repulsion at the interface
| Autor: | Masamichi Ikeguchi, Eriko Aoki |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0303 health sciences
Arginine Chemistry Protein subunit Biophysics Review 010402 general chemistry medicine.disease_cause 01 natural sciences Transmembrane protein Virulence factor 0104 chemical sciences Haemophilus influenzae Bacterial adhesin 03 medical and health sciences Transmembrane domain Structural Biology medicine Bacterial outer membrane Molecular Biology 030304 developmental biology |
| Zdroj: | Biophysical Reviews. 11:303-309 |
| ISSN: | 1867-2469 1867-2450 |
| DOI: | 10.1007/s12551-019-00535-0 |
| Popis: | Haemophilus influenzae adhesin (Hia) belongs to the trimeric autotransporter family, and it mediates the adherence of these bacteria to the epithelial cells of host organisms. Hia is composed of the passenger domain, which is a virulence factor, and the translocator domain, which anchors the passenger domain into the outer membrane. The Hia transmembrane domain forms a transmembrane β-barrel of 12 β-strands, four of which are provided from each subunit. The β-barrel has a pore that is traversed by three α-helices, one of which is provided from each subunit. This domain has a unique arginine arrangement inside the β-barrel. The side chains of the arginine residues protrude from the β-strands of three subunits toward the center of the barrel and are close to each other. Mutation of this arginine residue revealed the importance of the electrostatic repulsion between the three arginines. Electrostatic repulsion is considered to prevent misfolding and/or misassembly. The arginine clusters at the interface were found in several proteins and might generally play an important role in the assembly of the oligomer. |
| Databáze: | OpenAIRE |
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