title: Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase.
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.
authors.affiliation: MRC Cancer Cell Unit, Hutchison MRC Centre, Hills Road, Cambridge CB2 0XZ, United Kingdom.
authors.forename: Elizabeth R
authors.initials: ER
authors.lastname: Barry
authors.forename: Janet E
authors.initials: JE
authors.lastname: Lovett
authors.forename: Alessandro
authors.initials: A
authors.lastname: Costa
authors.forename: Susan M
authors.initials: SM
authors.lastname: Lea
authors.forename: Stephen D
authors.initials: SD
authors.lastname: Bell
mesh_terms: D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D017124:Conserved Sequence; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D009711:Nucleotides / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry* / Q000378:metabolism*; D017384:Sequence Deletion; D013329:Structure-Activity Relationship; D048229:Sulfolobus solfataricus / Q000201:enzymology*
chemical_list: D050505:Mutant Proteins; D009711:Nucleotides; D021122:Protein Subunits; D004265:DNA Helicases