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-Structure paper
Title | Structure of the eukaryotic MCM complex at 3.8 Å. |
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Journal, issue, pages | Nature, Vol. 524, Issue 7564, Page 186-191, Year 2015 |
Publish date | Aug 13, 2015 |
Authors | Ningning Li / Yuanliang Zhai / Yixiao Zhang / Wanqiu Li / Maojun Yang / Jianlin Lei / Bik-Kwoon Tye / Ning Gao / |
PubMed 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 ...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. |
External links | Nature / PubMed:26222030 |
Methods | EM (single particle) |
Resolution | 3.8 Å |
Structure data | |
Chemicals | ChemComp-ADP: |
Source |
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Keywords | HYDROLASE / Cryo-EM / single particle / MCM2-7 / DNA replication |