Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex
| Autor: | Christoph Wiedemann, Sabine Häfner, Anna Szambowska, Oliver Ohlenschläger, Matthias Görlach, Karl-Heinz Gührs |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Methanobacteriaceae Magnetic Resonance Spectroscopy Stereochemistry Archaeal Proteins Recombinant Fusion Proteins Molecular Sequence Data ved/biology.organism_classification_rank.species Winged Helix adenosine triphosphatases eukaryotic cell dna helicases chimera organism dna archaea sulfolobus helix (snails) Protein Structure Secondary Adenosine Triphosphate Minichromosome maintenance Structural Biology Genetics Amino Acid Sequence Peptide sequence Phylogeny Adenosine Triphosphatases Minichromosome Maintenance Proteins Sequence Homology Amino Acid biology ved/biology Hydrolysis Sulfolobus solfataricus DNA Helicases Helicase biology.organism_classification Protein Structure Tertiary Sulfolobus Biochemistry Mutation Helix biology.protein Linker |
| Zdroj: | Nucleic acids research, 43(5): 2958-2967 Nucleic Acids Research OpenAIRE Europe PubMed Central |
| Popis: | 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 ?-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 ?-helical linker element and by N-terminal residues of the first ?-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. |
| Databáze: | OpenAIRE |
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