Cholesterol catalyzes unfolding in membrane-inserted motifs of the pore forming protein cytolysin A.

ABSTRACT: Plasma membrane-induced protein folding and conformational transitions play a central role in cellular homeostasis. Several transmembrane proteins are folded in the complex lipid milieu to acquire a specific structure and function. Bacterial pore forming toxins (PFTs) are proteins expressed by a large class of pathogenic bacteria that exploit the plasma membrane environment to efficiently undergo secondary structure changes, oligomerize, and form transmembrane pores. Unregulated pore formation causes ion imbalance, leading to cell death and infection. Determining the free energy landscape of these membrane-driven-driven transitions remains a challenging problem. Although cholesterol recognition is required for lytic activity of several proteins in the PFT family of toxins, the regulatory r

SUBMITTER: Kulshrestha A 

PROVIDER: S-EPMC10598289 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature