Large-scale structure of RecA protein from Deinococcus radiodurance and its complexes in solution. Karelov, D., Lebedev, D., Suslov, A., Shalguev, V., Kuklin, A., Islamov, A., Lauter, H., Lanzov, V., & Isaev-Ivanov, V. Journal of Physics Condensed Matter, 2008. cited By 1![Large-scale structure of RecA protein from Deinococcus radiodurance and its complexes in solution [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Different conformational states of the filaments formed by RecA protein from a radiation resistant strain Deinococcus radiodurance (RecADr) in solution were investigated using small angle neutron scattering. Scattering by the protein self-polymer was consistent with a long helix model, with the pitch of the helix being lower than that in the crystal structure. Compared to those of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, helical filaments of RecA from D.radiodurance exhibited a lower helical pitch and lower stability at low Mg2+ concentrations or under conditions of elevated ionic strength in the absence of ATP (adenosine triphosphate). Formation of an active filament upon binding of ATPγS and either single-or double-stranded DNA brought about a significant increase in the helix pitch and a moderate decrease in the cross-sectional gyration radius, but resulted in little change in the number of monomers per helix turn. The helix pitch value of the RecA Dr presynaptic complex was conservative and close to that found for other RecA proteins and their analogs. © IOP Publishing Ltd.
@ARTICLE{Karelov2008,
author={Karelov, D.V. and Lebedev, D.V. and Suslov, A.V. and Shalguev, V.I. and Kuklin, A.I. and Islamov, A.Kh. and Lauter, H. and Lanzov, V.A. and Isaev-Ivanov, V.V.},
title={Large-scale structure of RecA protein from Deinococcus radiodurance and its complexes in solution},
journal={Journal of Physics Condensed Matter},
year={2008},
volume={20},
number={10},
doi={10.1088/0953-8984/20/10/104215},
art_number={104215},
note={cited By 1},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-41849107564&doi=10.1088%2f0953-8984%2f20%2f10%2f104215&partnerID=40&md5=ad0548b44c3c670e7599d7037610244b},
affiliation={Petersburg Nuclear Physics Institute, Gatchina, Russian Federation; Joint Institute for Nuclear Research, Dubna, Russian Federation; Institute Max von Laue Paul Langevin, Grenoble, France},
abstract={Different conformational states of the filaments formed by RecA protein from a radiation resistant strain Deinococcus radiodurance (RecADr) in solution were investigated using small angle neutron scattering. Scattering by the protein self-polymer was consistent with a long helix model, with the pitch of the helix being lower than that in the crystal structure. Compared to those of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, helical filaments of RecA from D.radiodurance exhibited a lower helical pitch and lower stability at low Mg2+ concentrations or under conditions of elevated ionic strength in the absence of ATP (adenosine triphosphate). Formation of an active filament upon binding of ATPγS and either single-or double-stranded DNA brought about a significant increase in the helix pitch and a moderate decrease in the cross-sectional gyration radius, but resulted in little change in the number of monomers per helix turn. The helix pitch value of the RecA Dr presynaptic complex was conservative and close to that found for other RecA proteins and their analogs. © IOP Publishing Ltd.},
correspondence_address1={Karelov, D. V.; Petersburg Nuclear Physics Institute, Gatchina, Russian Federation},
issn={09538984},
coden={JCOME},
language={English},
abbrev_source_title={J Phys Condens Matter},
document_type={Article},
source={Scopus},
}
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