Abstract
The crystal structure of the N-terminal domain of the Pyrococcus furiosus minichromosome maintenance (MCM) protein as a double hexamer is described. The MCM complex is a ring-shaped helicase that unwinds DNA at the replication fork of eukaryotes and archaea. Prior to replication initiation, the MCM complex assembles as an inactive double hexamer at specific sites of DNA. The presented structure is highly consistent with previous MCM double-hexamer structures and shows two MCM hexamers with a head-to-head interaction mediated by the N-terminal domain. Minor differences include a diminished head-to-head interaction and a slightly reduced inter-hexamer rotation.
Keywords:
DNA replication; MCM; Pyrococcus furiosus; helicase; minichromosome maintenance.
MeSH terms
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Amino Acid Sequence
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / metabolism
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Binding Sites
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Cations, Divalent
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Cloning, Molecular
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Crystallography, X-Ray
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DNA Replication
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DNA, Archaeal / chemistry*
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DNA, Archaeal / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Kinetics
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Minichromosome Maintenance Proteins / chemistry*
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Minichromosome Maintenance Proteins / genetics
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Minichromosome Maintenance Proteins / metabolism
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Models, Molecular
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Plasmids / chemistry
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Plasmids / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Protein Multimerization
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Pyrococcus furiosus / chemistry*
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Pyrococcus furiosus / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
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Zinc / chemistry*
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Zinc / metabolism
Substances
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Archaeal Proteins
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Cations, Divalent
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DNA, Archaeal
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Recombinant Proteins
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Minichromosome Maintenance Proteins
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Zinc