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Tetrameric structure of thermostable direct hemolysin from vibrio parahaemolyticus revealed by ultracentrifugation, small-angle X-ray scattering and electron microscopy.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Hamada D,Higurashi T,Mayanagi K,Miyata T,Fukui T,Iida T,Honda T,Yanagihara I

doi

10.1016/j.jmb.2006.09.070

subject

Has Abstract

pub_date

2007-01-05 00:00:00

pages

187-95

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(06)01294-0

journal_volume

365

pub_type

杂志文章

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