Analytical model for determination of parameters of helical structures in solution by small angle scattering: comparison of RecA structures by SANS

FEBS Lett. 2003 Feb 27;537(1-3):182-6. doi: 10.1016/s0014-5793(03)00107-8.

Abstract

The filament structures of the self-polymers of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, their complexes with ATPgammaS, phage M13 single-stranded DNA (ssDNA) and the tertiary complexes RecA::ATPgammaS::ssDNA were compared by small angle neutron scattering. A model was developed that allowed for an analytical solution for small angle scattering on a long helical filament, making it possible to obtain the helical pitch and the mean diameter of the protein filament from the scattering curves. The results suggest that the structure of the filaments formed by these two RecA proteins, and particularly their complexes with ATPgammaS, is conservative.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives*
  • Adenosine Triphosphate / chemistry
  • Bacterial Proteins / chemistry
  • Binding Sites
  • DNA, Single-Stranded / chemistry
  • Escherichia coli / chemistry
  • Escherichia coli Proteins / chemistry
  • Models, Theoretical
  • Protein Structure, Secondary
  • Pseudomonas aeruginosa / chemistry
  • Rec A Recombinases / chemistry*
  • Scattering, Radiation
  • Spectrum Analysis

Substances

  • Bacterial Proteins
  • DNA, Single-Stranded
  • Escherichia coli Proteins
  • adenosine 5'-O-(3-thiotriphosphate)
  • Adenosine Triphosphate
  • Rec A Recombinases