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Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N‐terminal domain
Author(s) -
Meagher Martin,
Enemark Eric J.
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1600858x
Subject(s) - random hexamer , minichromosome maintenance , pyrococcus furiosus , helicase , seqa protein domain , crystallography , dna replication , biology , chemistry , dna , stereochemistry , genetics , origin of replication , archaea , gene , rna
The crystal structure of the N‐terminal domain of the Pyrococcus furiosus minichromosome maintenance (MCM) protein as a double hexamer is described. The MCM complex is a ring‐shaped helicase that unwinds DNA at the replication fork of eukaryotes and archaea. Prior to replication initiation, the MCM complex assembles as an inactive double hexamer at specific sites of DNA. The presented structure is highly consistent with previous MCM double‐hexamer structures and shows two MCM hexamers with a head‐to‐head interaction mediated by the N‐terminal domain. Minor differences include a diminished head‐to‐head interaction and a slightly reduced inter‐hexamer rotation.