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

• Sugawara, Takaki

• Yamashita, Daichi

• Tanaka, Yoshikazu

• Kaneko, Jun

• Kamio, Yoshiyuki

• Tanaka, Isao

• Yao, Min

抄録

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.

収録刊行物

• Acta Crystallographica Section F : Structural Biology and Crystallization Communications

  Acta Crystallographica Section F : Structural Biology and Crystallization Communications 69 (8), 868-870, 2013-08

  International Union of Crystallography

キーワード

• staphylococcal
• alpha-haemolysin
• monomer
• pore-forming toxins

詳細情報

• CRID: 1050845763944560128
• NII論文ID: 120005317012
• HANDLE: 2115/53113
• ISSN: 17443091
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles