1QOY

E.coli Hemolysin E (HlyE, ClyA, SheA)

Summary for 1QOY

• Entry DOI: 10.2210/pdb1qoy/pdb
• Descriptor: HEMOLYSIN E, SULFATE ION (3 entities in total)
• Functional Keywords: toxin, membrane pore former, cytolysin, hemolysin, pores
• Biological source: ESCHERICHIA COLI
• Cellular location: Secreted: P77335
• Total number of polymer chains: 1
• Total formula weight: 35101.77

Authors

Wallace, A.J.,Stillman, T.J.,Atkins, A.,Jamieson, S.J.,Bullough, P.A.,Green, J.,Artymiuk, P.J. (deposition date: 1999-11-25, release date: 2000-01-23, Last modification date: 2024-05-08)

Primary citation

Wallace, A.J.,Stillman, T.J.,Atkins, A.,Jamieson, S.J.,Bullough, P.A.,Green, J.,Artymiuk, P.J.
E. Coli Hemolysin E (Hlye, Clya, Shea): X-Ray Crystal Structure of the Toxin and Observation of Membrane Pores by Electron Microscopy
Cell(Cambridge,Mass.), 100:265-, 2000

PubMed 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.

PubMed: 10660049
DOI: 10.1016/S0092-8674(00)81564-0

Experimental method

X-RAY DIFFRACTION (2 Å)