Ontology highlight
ABSTRACT:
SUBMITTER: Piller P
PROVIDER: S-EPMC10153742 | biostudies-literature | 2023 May
REPOSITORIES: biostudies-literature
Piller Paulina P Semeraro Enrico F EF Rechberger Gerald N GN Keller Sandro S Pabst Georg G
PNAS nexus 20230411 5
The activity of integral membrane proteins is tightly coupled to the properties of the surrounding lipid matrix. In particular, transbilayer asymmetry, a hallmark of all plasma membranes, might be exploited to control membrane-protein activity. Here, we hypothesized that the membrane-embedded enzyme outer membrane phospholipase A (OmpLA) is susceptible to the lateral pressure differences that build up between such asymmetric membrane leaflets. Upon reconstituting OmpLA into synthetic, chemically ...[more]