open access

https://hdl.handle.net/2115/53113

Preliminary X-ray crystallographic study of staphylococcal alpha-haemolysin monomer

英語

pore-forming toxins

2013-08

International Union of Crystallography

Acta Crystallographica Section F : Structural Biology and Crystallization Communications

69(8)

868-870

Staphylococcal alpha-haemolysin is a beta-barrel pore-forming toxin expressed by Staphylococcus aureus. alpha-Haemolysin is secreted as a water-soluble monomeric protein which binds to target membranes and forms membrane-inserted heptameric pores. Although the crystal structures of the heptameric pore and monomer bound to an antibody have been determined, that of monomeric alpha-haemolysin without binder has yet to be elucidated. Previous mutation studies showed that mutants of His35 retain the monomeric structure but are unable to assemble into heptamers. Here, alpha-haemolysin H35A mutants were expressed, purified and crystallized. Diffraction data were collected to 2.90 angstrom resolution. The crystals belonged to space group P6(1), with unit-cell parameters a = b = 151.3, c = 145.0 angstrom. Molecular replacement found four molecules in an asymmetric unit. The relative orientation among molecules was distinct from that of the pore, indicating that the crystal contained monomeric alpha-haemolysin.

学術雑誌論文

Version of Record

1744-3091