Structure of the eukaryotic MCM complex at 3.8 Å View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-08

AUTHORS

Ningning Li, Yuanliang Zhai, Yixiao Zhang, Wanqiu Li, Maojun Yang, Jianlin Lei, Bik-Kwoon Tye, Ning Gao

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. More... »

PAGES

186

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nature14685

    DOI

    http://dx.doi.org/10.1038/nature14685

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1039721868

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26222030


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