Journal
NUCLEIC ACIDS RESEARCH
Volume 36, Issue 10, Pages 3235-3243Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkn183
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- Medical Research Council [G0500367] Funding Source: researchfish
- Medical Research Council [G0500367] Funding Source: Medline
- MRC [G0500367] Funding Source: UKRI
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The Mini-Chromosome Maintenance (MCM) proteins are candidates of replicative DNA helicase in eukarya and archaea. Here we report a 2.8 crystal structure of the N-terminal domain (residues 1268) of the Sulfolobus solfataricus MCM (Sso MCM) protein. The structure reveals single-hexameric ring-like architecture, at variance from the protein of Methanothermobacter thermoautotrophicus (Mth). Moreover, the central channel in Sso MCM seems significantly narrower than the Mth counterpart, which appears to more favorably accommodate single-stranded DNA than double-stranded DNA, as supported by DNA-binding assays. Structural analysis also highlights the essential role played by the zinc-binding domain in the interaction with nucleic acids and allows us to speculate that the Sso MCM N-ter domain may function as a molecular clamp to grasp the single-stranded DNA passing through the central channel. On this basis possible DNA unwinding mechanisms are discussed.
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