E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy
| Autor: | A J, Wallace, T J, Stillman, A, Atkins, S J, Jamieson, P A, Bullough, J, Green, P J, Artymiuk |
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| Rok vydání: | 2000 |
| Předmět: |
Sequence Homology
Amino Acid Escherichia coli Proteins Bacterial Toxins Molecular Sequence Data Membrane Proteins Porins Salmonella typhi Crystallography X-Ray Lipids Protein Structure Secondary Protein Structure Tertiary Shigella flexneri Hemolysin Proteins Microscopy Electron Bacterial Proteins Escherichia coli Protein Structure Quaternary Conserved Sequence |
| Zdroj: | Cell. 100(2) |
| ISSN: | 0092-8674 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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