| Literature DB >> 19164574 |
Elizabeth R Barry1, Janet E Lovett, Alessandro Costa, Susan M Lea, Stephen D Bell.
Abstract
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.Entities:
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Year: 2009 PMID: 19164574 PMCID: PMC2633543 DOI: 10.1073/pnas.0809192106
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205