5iy0

Publication Abstract from PubMed

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.

Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain.,Meagher M, Enemark EJ Acta Crystallogr F Struct Biol Commun. 2016 Jul 1;72(Pt 7):545-51. doi:, 10.1107/S2053230X1600858X. Epub 2016 Jun 22. PMID:27380371^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.