Characterization of lipid–protein interactions and lipid-mediated modulation of membrane protein function through molecular simulation

MP Muller, T Jiang, C Sun, M Lihan, S Pant… - Chemical …, 2019 - ACS Publications
The cellular membrane constitutes one of the most fundamental compartments of a living
cell, where key processes such as selective transport of material and exchange of …

The Genetics and Cell Biology of Wolbachia-Host Interactions

LR Serbus, C Casper-Lindley… - Annual review of …, 2008 - annualreviews.org
Wolbachia are gram-negative bacteria that are widespread in nature, carried by the majority
of insect species as well as some mites, crustaceans, and filarial nematodes. Wolbachia can …

Outer membrane proteins of Pasteurella multocida

T Hatfaludi, K Al-Hasani, JD Boyce, B Adler - Veterinary microbiology, 2010 - Elsevier
Pasteurella multocida is a ubiquitous pathogen which causes a range of diseases in diverse
animal species. Components of the bacterial outer membrane, such as trans membrane …

OmpA: a flexible clamp for bacterial cell wall attachment

F Samsudin, ML Ortiz-Suarez, TJ Piggot, PJ Bond… - Structure, 2016 - cell.com
The envelope of Gram-negative bacteria is highly complex, containing separate outer and
inner membranes and an intervening periplasmic space encompassing a peptidoglycan …

Binding from both sides: TolR and full-length OmpA bind and maintain the local structure of the E. coli cell wall

AT Boags, F Samsudin, S Khalid - Structure, 2019 - cell.com
We present a molecular modeling and simulation study of the E. coli cell envelope, with a
particular focus on the role of TolR, a native protein of the E. coli inner membrane, in …

Full-length OmpA: structure, function, and membrane interactions predicted by molecular dynamics simulations

ML Ortiz-Suarez, F Samsudin, TJ Piggot, PJ Bond… - Biophysical journal, 2016 - cell.com
OmpA is a multidomain protein found in the outer membranes of most Gram-negative
bacteria. Despite a wealth of reported structural and biophysical studies, the structure …

Vaccination with Pasteurella multocida recombinant OmpA induces strong but non-protective and deleterious Th2-type immune response in mice

SM Dabo, A Confer, M Montelongo, P York… - Vaccine, 2008 - Elsevier
Pasteurella multocida OmpA (PmOmpA) belongs to the major and multifunctional
Escherichia coli OmpA family of proteins. We have previously reported that the protein is …

Presence of substrate aids lateral gate separation in LptD

KP Lundquist, JC Gumbart - Biochimica et Biophysica Acta (BBA) …, 2020 - Elsevier
Lipopolysaccharides (LPS) provide the outer membrane (OM) of Gram-negative bacteria
with a strong protective barrier. The periplasm-spanning Lpt machinery is responsible for the …

Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers

N Mohseni Sani, M Talaee, A Akbari… - Microbiology …, 2024 - Am Soc Microbiol
The emulsifying ability of SA01-OmpA (outer membrane protein A from Acinetobacter sp.
SA01) was found to be constrained by challenges like low production efficiency and high …

Atomistic molecular-dynamics simulations enable prediction of the arginine permeation pathway through OccD1/OprD from Pseudomonas aeruginosa

J Parkin, S Khalid - Biophysical journal, 2014 - cell.com
Pseudomonas aeruginosa is a Gram-negative bacterium that does not contain large,
nonspecific porins in its outer membrane. Consequently, the outer membrane is highly …