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Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain.

ABSTRACT: 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.

SUBMITTER: Meagher M

PROVIDER: S-EPMC4933004 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain.

Meagher Martin M Enemark Eric J EJ

Acta crystallographica. Section F, Structural biology communications 20160622 Pt 7

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 hea ...[more]

PMID: 27380371

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