2VL6

STRUCTURAL ANALYSIS OF THE SULFOLOBUS SOLFATARICUS MCM PROTEIN N- TERMINAL DOMAIN

Summary for 2VL6

• Entry DOI: 10.2210/pdb2vl6/pdb
• Descriptor: MINICHROMOSOME MAINTENANCE PROTEIN MCM, ZINC ION (3 entities in total)
• Functional Keywords: mcm, helicase, hydrolase, zinc-finger, atp-binding, dna-binding, ssdna binding, dna replication, nucleotide-binding, dna binding protein
• Biological source: SULFOLOBUS SOLFATARICUS
• Total number of polymer chains: 3
• Total formula weight: 93625.59

Authors

Liu, W.,Pucci, B.,Rossi, M.,Pisani, F.M.,Ladenstein, R. (deposition date: 2008-01-08, release date: 2008-04-29, Last modification date: 2023-12-13)

Primary citation

Liu, W.,Pucci, B.,Rossi, M.,Pisani, F.M.,Ladenstein, R.
Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain.
Nucleic Acids Res., 36:3235-, 2008

PubMed Abstract: 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.

PubMed: 18417534
DOI: 10.1093/NAR/GKN183

Experimental method

X-RAY DIFFRACTION (2.8 Å)