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

Journal Article · Wed Jun 22 04:00:00 EDT 2016 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X1600858X· OSTI ID:1260841

Meagher, Martin; Enemark, Eric J.

The crystal structure of the N-terminal domain of thePyrococcus furiosusminichromosome 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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: OTHERNIGMS
• OSTI ID: 1260841
• Journal Information: Acta Crystallographica. Section F, Structural Biology Communications, Journal Name: Acta Crystallographica. Section F, Structural Biology Communications Journal Issue: 7 Vol. 72; ISSN 2053-230X
• Publisher: International Union of Crystallography
• Country of Publication: United States
• Language: ENGLISH