2vl6
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Revision as of 10:24, 30 April 2008
STRUCTURAL ANALYSIS OF THE SULFOLOBUS SOLFATARICUS MCM PROTEIN N-TERMINAL DOMAIN
Overview
The Mini-Chromosome Maintenance (MCM) proteins are candidates of replicative DNA helicase in eukarya and archaea. Here we report a 2.8 A 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.
About this Structure
2VL6 is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain{dagger}, Liu W, Pucci B, Rossi M, Pisani FM, Ladenstein R, Nucleic Acids Res. 2008 Apr 16;. PMID:18417534 Page seeded by OCA on Wed Apr 30 13:24:14 2008
