The solution structure of full-length dodecameric MCM by SANS and molecular modeling.

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 Mg(2+) 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.