RRC ID 3140
著者 Hamada D, Higurashi T, Mayanagi K, Miyata T, Fukui T, Iida T, Honda T, Yanagihara I.
タイトル Tetrameric structure of thermostable direct hemolysin from vibrio parahaemolyticus revealed by ultracentrifugation, small-angle X-ray scattering and electron microscopy.
ジャーナル J Mol Biol
Abstract The thermostable direct hemolysin (TDH) is a major virulence factor of Vibrio parahaemolyticus. We have characterized the conformational properties of TDH by small-angle X-ray scattering (SAXS), ultracentrifugation and transmission electron microscopy. Sedimentation equilibrium and velocity studies revealed that the protein is tetrameric in aqueous solvents. The Guinier plot derived from SAXS data provided a radius of gyration of 29.0 A. The elongated pattern with a shoulder of a pair distance distribution function derived from SAXS data suggested the presence of molecules with an anisotropic shape having a maximum diameter of 98 A. Electron microscopic image analysis of the negatively stained TDH oligomer showed the presence of C(4) symmetric particles with edge and diagonal lengths of 65 A and 80 A, respectively. Shape reconstruction was carried out by ab initio calculations using the SAXS data with a C(4) symmetric approximation. These results suggested that the tetrameric TDH assumes an oblate structure. The hydrodynamic parameters predicted from the ab initio model differed slightly from the experimental values, suggesting the presence of flexible segments.
巻・号 365(1)
ページ 187-95
公開日 2007-1-5
DOI 10.1016/j.jmb.2006.09.070
PII S0022-2836(06)01294-0
PMID 17056060
MeSH Bacterial Toxins / chemistry Hemolysin Proteins / chemistry* Microscopy, Electron, Transmission Models, Molecular Protein Structure, Quaternary Scattering, Small Angle Ultracentrifugation Vibrio parahaemolyticus / chemistry* Vibrio parahaemolyticus / pathogenicity Virulence Factors X-Rays
IF 4.76
引用数 17
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
病原微生物