Full-Length OmpA: Structure, Function, and Membrane Interactions Predicted by Molecular Dynamics Simulations.

ABSTRACT: 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-function relationships of this protein remain unclear. For example, it is still debated whether it functions as a pore, and the precise molecular role it plays in attachment to the peptidoglycan of the periplasm is unknown. The absence of a consensus view is partly due to the lack of a complete structure of the full-length protein. To address this issue, we performed molecular-dynamics simulations of the full-length model of the OmpA dimer proposed by Robinson and co-workers. The N-terminal domains were embedded in an asymmetric model of the outer membrane, with lipopolysaccharide molecules in the outer leaflet and phospho

SUBMITTER: Ortiz-Suarez ML 

PROVIDER: S-EPMC5071624 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature