2VL6

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

2VL6 の概要

• エントリーDOI: 10.2210/pdb2vl6/pdb
• 分子名称: MINICHROMOSOME MAINTENANCE PROTEIN MCM, ZINC ION (3 entities in total)
• 機能のキーワード: mcm, helicase, hydrolase, zinc-finger, atp-binding, dna-binding, ssdna binding, dna replication, nucleotide-binding, dna binding protein
• 由来する生物種: SULFOLOBUS SOLFATARICUS
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 93625.59

構造登録者

Liu, W.,Pucci, B.,Rossi, M.,Pisani, F.M.,Ladenstein, R. (登録日: 2008-01-08, 公開日: 2008-04-29, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)