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- W2073669903 abstract "The minichromosome maintenance complex (MCM) represents the replicative DNA helicase both in eukaryotes and archaea. Here, we describe the solution structure of the C-terminal domains of the archaeal MCMs of Sulfolobus solfataricus (Sso) and Methanothermobacter thermautotrophicus (Mth). Those domains consist of a structurally conserved truncated winged helix (WH) domain lacking the two typical ‘wings’ of canonical WH domains. A less conserved N-terminal extension links this WH module to the MCM AAA+ domain forming the ATPase center. In the Sso MCM this linker contains a short α-helical element. Using Sso MCM mutants, including chimeric constructs containing Mth C-terminal domain elements, we show that the ATPase and helicase activity of the Sso MCM is significantly modulated by the short α-helical linker element and by N-terminal residues of the first α-helix of the truncated WH module. Finally, based on our structural and functional data, we present a docking-derived model of the Sso MCM, which implies an allosteric control of the ATPase center by the C-terminal domain." @default.
- W2073669903 created "2016-06-24" @default.
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- W2073669903 date "2015-02-20" @default.
- W2073669903 modified "2023-10-10" @default.
- W2073669903 title "Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex" @default.
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- W2073669903 doi "https://doi.org/10.1093/nar/gkv120" @default.
- W2073669903 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4357721" @default.
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- W2073669903 hasPublicationYear "2015" @default.
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