| Literature DB >> 10660049 |
A J Wallace1, T J Stillman, A Atkins, S J Jamieson, P A Bullough, J Green, P J Artymiuk.
Abstract
Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal structure of the water-soluble form of E. coli HlyE at 2.0 A resolution and the visualization of the lipid-associated form of the toxin in projection at low resolution by electron microscopy. The crystal structure reveals HlyE to be the first member of a new family of toxin structures, consisting of an elaborated helical bundle some 100 A long. The electron micrographs show how HlyE oligomerizes in the presence of lipid to form transmembrane pores. Taken together, the data from these two structural techniques allow us to propose a simple model for the structure of the pore and for membrane interaction.Entities:
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Year: 2000 PMID: 10660049 DOI: 10.1016/s0092-8674(00)81564-0
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582