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Structure of the eukaryotic MCM complex at 3.8 Å

Author

Listed:
  • Ningning Li

    (Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Yuanliang Zhai

    (Hong Kong Universityof Science and Technology
    Institute for Advanced Study, Hong Kong University of Science and Technology)

  • Yixiao Zhang

    (Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Wanqiu Li

    (Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Maojun Yang

    (Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Jianlin Lei

    (Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Bik-Kwoon Tye

    (Hong Kong Universityof Science and Technology
    College of Agriculture and Life Sciences, Cornell University)

  • Ning Gao

    (Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University)

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.

Suggested Citation

  • Ningning Li & Yuanliang Zhai & Yixiao Zhang & Wanqiu Li & Maojun Yang & Jianlin Lei & Bik-Kwoon Tye & Ning Gao, 2015. "Structure of the eukaryotic MCM complex at 3.8 Å," Nature, Nature, vol. 524(7564), pages 186-191, August.
    • Handle: RePEc:nat:nature:v:524:y:2015:i:7564:d:10.1038_nature14685
    DOI: 10.1038/nature14685
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