Structure of the eukaryotic MCM complex at 3.8 Å.

Abstract:

:DNA replication in eukaryotes is strictly regulated by several mechanisms. A central step in this replication is the assembly of the heterohexameric minichromosome maintenance (MCM2-7) helicase complex at replication origins during G1 phase as an inactive double hexamer. Here, using cryo-electron microscopy, we report a near-atomic structure of the MCM2-7 double hexamer purified from yeast G1 chromatin. Our structure shows that two single hexamers, arranged in a tilted and twisted fashion through interdigitated amino-terminal domain interactions, form a kinked central channel. Four constricted rings consisting of conserved interior β-hairpins from the two single hexamers create a narrow passageway that tightly fits duplex DNA. This narrow passageway, reinforced by the offset of the two single hexamers at the double hexamer interface, is flanked by two pairs of gate-forming subunits, MCM2 and MCM5. These unusual features of the twisted and tilted single hexamers suggest a concerted mechanism for the melting of origin DNA that requires structural deformation of the intervening DNA.

journal_name

Nature

journal_title

Nature

authors

Li N,Zhai Y,Zhang Y,Li W,Yang M,Lei J,Tye BK,Gao N

doi

10.1038/nature14685

subject

Has Abstract

pub_date

2015-08-13 00:00:00

pages

186-91

issue

7564

eissn

0028-0836

issn

1476-4687

pii

nature14685

journal_volume

524

pub_type

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