The solution structure of full-length dodecameric MCM by SANS and molecular modeling. Krueger, S., Shin, J., Curtis, J. E., Rubinson, K. A., & Kelman, Z. Proteins: Structure, Function, and Bioinformatics, 82(10):2364–2374, 2014. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24598![The solution structure of full-length dodecameric MCM by SANS and molecular modeling [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The solution structure of the full-length DNA helicase minichromosome maintenance protein from Methanothermobacter thermautotrophicus was determined by small-angle neutron scattering (SANS) data together with all-atom molecular modeling. The data were fit best with a dodecamer (dimer of hexamers). The 12 monomers were linked together by the B/C domains, and the adenosine triphosphatase (AAA+) catalytic regions were found to be freely movable in the full-length dodecamer both in the presence and absence of Mg2+ and 50-meric single-stranded DNA (ssDNA). In particular, the SANS data and molecular modeling indicate that all 12 AAA+ domains in the dodecamer lie approximately the same distance from the axis of the molecule, but the positions of the helix–turn–helix region at the C-terminus of each monomer differ. In addition, the A domain at the N-terminus of each monomer is tucked up next to the AAA+ domain for all 12 monomers of the dodecamer. Finally, binding of ssDNA does not lock the AAA+ domains in any specific position, which leaves them with the flexibility to move both for helicase function and for binding along the ssDNA. Proteins 2014; 82:2364–2374. © 2014 Wiley Periodicals, Inc.
@article{krueger_solution_2014,
title = {The solution structure of full-length dodecameric {MCM} by {SANS} and molecular modeling},
volume = {82},
copyright = {© 2014 Wiley Periodicals, Inc.},
issn = {1097-0134},
url = {http://onlinelibrary.wiley.com/doi/abs/10.1002/prot.24598},
doi = {10.1002/prot.24598},
abstract = {The solution structure of the full-length DNA helicase minichromosome maintenance protein from Methanothermobacter thermautotrophicus was determined by small-angle neutron scattering (SANS) data together with all-atom molecular modeling. The data were fit best with a dodecamer (dimer of hexamers). The 12 monomers were linked together by the B/C domains, and the adenosine triphosphatase (AAA+) catalytic regions were found to be freely movable in the full-length dodecamer both in the presence and absence of Mg2+ and 50-meric single-stranded DNA (ssDNA). In particular, the SANS data and molecular modeling indicate that all 12 AAA+ domains in the dodecamer lie approximately the same distance from the axis of the molecule, but the positions of the helix–turn–helix region at the C-terminus of each monomer differ. In addition, the A domain at the N-terminus of each monomer is tucked up next to the AAA+ domain for all 12 monomers of the dodecamer. Finally, binding of ssDNA does not lock the AAA+ domains in any specific position, which leaves them with the flexibility to move both for helicase function and for binding along the ssDNA. Proteins 2014; 82:2364–2374. © 2014 Wiley Periodicals, Inc.},
language = {en},
number = {10},
urldate = {2020-05-02},
journal = {Proteins: Structure, Function, and Bioinformatics},
author = {Krueger, Susan and Shin, Jae-Ho and Curtis, Joseph E. and Rubinson, Kenneth A. and Kelman, Zvi},
year = {2014},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24598},
keywords = {DNA helicase, DNA replication, Monte Carlo simulations, minichromosome maintenance protein, small-angle neutron scattering},
pages = {2364--2374}
}
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