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3JA8

Cryo-EM structure of the MCM2-7 double hexamer

Summary for 3JA8
Entry DOI10.2210/pdb3ja8/pdb
EMDB information6338
DescriptorMinichromosome Maintenance 2, Minichromosome Maintenance 3, Minichromosome Maintenance 4, ... (7 entities in total)
Functional Keywordscryo-em, single particle, mcm2-7, dna replication, hydrolase
Biological sourceSaccharomyces cerevisiae S288c (yeast)
More
Total number of polymer chains6
Total formula weight608932.45
Authors
Li, N.,Zhai, Y.,Zhang, Y.,Li, W.,Yang, M.,Lei, J.,Tye, B.K.,Gao, N. (deposition date: 2015-05-09, release date: 2015-08-05, Last modification date: 2024-03-20)
Primary citationLi, N.,Zhai, Y.,Zhang, Y.,Li, W.,Yang, M.,Lei, J.,Tye, B.K.,Gao, N.
Structure of the eukaryotic MCM complex at 3.8 angstrom
Nature, 524:186-191, 2015
Cited by
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 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.
PubMed: 26222030
DOI: 10.1038/nature14685
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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