HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >

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

Files in This Item:
sendreprint.pdf256.72 kBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Preliminary X-ray crystallographic study of staphylococcal alpha-haemolysin monomer
Authors: Sugawara, Takaki Browse this author
Yamashita, Daichi Browse this author
Tanaka, Yoshikazu Browse this author →KAKEN DB
Kaneko, Jun Browse this author →KAKEN DB
Kamio, Yoshiyuki Browse this author →KAKEN DB
Tanaka, Isao Browse this author →KAKEN DB
Yao, Min Browse this author →KAKEN DB
Keywords: staphylococcal
pore-forming toxins
Issue Date: Aug-2013
Publisher: International Union of Crystallography
Journal Title: Acta Crystallographica Section F : Structural Biology and Crystallization Communications
Volume: 69
Issue: 8
Start Page: 868
End Page: 870
Publisher DOI: 10.1107/S174430911301693X
Abstract: 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.
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田中 良和

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 - Hokkaido University