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The minichromosome maintenance (MCM) helicase is the presumptive replicative helicase in archaea and eukaryotes. The archaeal homomultimeric MCM has a two-tier structure. One tier contains the AAA+ motor domains of the proteins, and these are the minimal functional helicase domains. The second tier is formed by the N-terminal domains. These domains are not essential for MCM helicase activity but act to enhance the processivity of the helicase. We reveal that a conserved loop facilitates communication between processivity and motor tiers. Interestingly, this allostery seems to be mediated by interactions between, rather than within, individual protomers in the MCM ring.

Original publication




Journal article


Proc Natl Acad Sci U S A

Publication Date





1051 - 1056


Allosteric Regulation, Amino Acid Sequence, Conserved Sequence, DNA Helicases, Models, Biological, Molecular Sequence Data, Mutant Proteins, Nucleotides, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Sequence Deletion, Structure-Activity Relationship, Sulfolobus solfataricus