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]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}
}

Downloads: 0