The electrostatic core of the outer membrane protein X from E. coli.
Coulomb interactions
Membrane protein folding
Protein stability
SDS-PAGE
Salt-bridge cluster
Thermal unfolding
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 01 2020
01 01 2020
Historique:
received:
02
04
2019
revised:
16
06
2019
accepted:
25
07
2019
pubmed:
3
8
2019
medline:
28
4
2020
entrez:
3
8
2019
Statut:
ppublish
Résumé
Electrostatic side chain contacts can contribute substantial interaction energy terms to the stability of proteins. The impact of electrostatic interactions on the structure and architecture of outer membrane proteins is however not well studied compared to soluble proteins. Here, we report the results of a systematic study of all charged side chains of the E. coli outer membrane protein X (OmpX). The data identify three distinct salt-bridge clusters in the core of OmpX that contribute significantly to protein stability in dodecylphosphocholine detergent micelles. The three clusters form an "electrostatic core" of the membrane protein OmpX, corresponding in its architectural role to the hydrophobic core of soluble proteins. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.
Identifiants
pubmed: 31374213
pii: S0005-2736(19)30177-4
doi: 10.1016/j.bbamem.2019.183031
pii:
doi:
Substances chimiques
Bacterial Outer Membrane Proteins
0
Escherichia coli Proteins
0
Micelles
0
OmpX protein, E coli
134632-13-6
Hydrolases
EC 3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
183031Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.