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

The filament structures of the self-polymers of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, their complexes with ATPγS, phage M13 single-stranded DNA (ssDNA) and the tertiary complexes RecA::ATPγS::ssDNA were compared by small angle neutron scattering. A model was developed that...

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Veröffentlicht in:	FEBS letters 2003-02, Vol.537 (1-3), p.182-186
Hauptverfasser:	Lebedev, D.V., Baitin, D.M., Islamov, A.Kh, Kuklin, A.I., Shalguev, V.Kh, Lanzov, V.A., Isaev-Ivanov, V.V.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - chemistry Bacterial Proteins - chemistry Binding Sites DNA, Single-Stranded - chemistry double-stranded DNA dsDNA Escherichia coli - chemistry Escherichia coli Proteins - chemistry Homologous recombination Models, Theoretical Protein Structure, Secondary Pseudomonas aeruginosa Pseudomonas aeruginosa - chemistry Rec A Recombinases - chemistry RecA protein SANS Scattering, Radiation single-stranded DNA Small angle neutron scattering Spectrum Analysis ssDNA
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Zusammenfassung:	The filament structures of the self-polymers of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, their complexes with ATPγS, phage M13 single-stranded DNA (ssDNA) and the tertiary complexes RecA::ATPγS::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 ATPγS, is conservative.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(03)00107-8