Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain

Wei Liu, Biagio Pucci, Mosè Rossi, Francesca M. Pisani, Rudolf Ladenstein

Research output: Contribution to journalArticle

Abstract

The Mini-Chromosome Maintenance (MCM) proteins are candidates of replicative DNA helicase in eukarya and archaea. Here we report a 2.8 Å crystal structure of the N-terminal domain (residues 1-268) 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.

Original languageEnglish
Pages (from-to)3235-3243
Number of pages9
JournalNucleic Acids Research
Volume36
Issue number10
DOIs
Publication statusPublished - Jun 2008

ASJC Scopus subject areas

  • Genetics

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    Liu, W., Pucci, B., Rossi, M., Pisani, F. M., & Ladenstein, R. (2008). Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain. Nucleic Acids Research, 36(10), 3235-3243. https://doi.org/10.1093/nar/gkn183