The Crystal Structure of Pneumolysin at 2.0 A Resolution Reveals the Molecular Packing of the Pre-pore Complex.

ABSTRACT: Pneumolysin is a cholesterol-dependent cytolysin (CDC) and virulence factor of Streptococcus pneumoniae. It kills cells by forming pores assembled from oligomeric rings in cholesterol-containing membranes. Cryo-EM has revealed the structures of the membrane-surface bound pre-pore and inserted-pore oligomers, however the molecular contacts that mediate these oligomers are unknown because high-resolution information is not available. Here we have determined the crystal structure of full-length pneumolysin at 1.98 Å resolution. In the structure, crystal contacts demonstrate the likely interactions that enable polymerisation on the cell membrane and the molecular packing of the pre-pore complex. The hemolytic activity is abrogated in mutants that disrupt these intermolecular contacts, highligh

SUBMITTER: Marshall JE 

PROVIDER: S-EPMC4558608 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature