Abstract
The DNA replication factor minichromosome maintenance 10 (MCM10) is a conserved, abundant nuclear protein crucial for origin firing. During the transition from pre-replicative complexes to pre-initiation complexes, MCM10 recruitment to replication origins is required to provide a physical link between the MCM2-7 complex DNA helicase and DNA polymerases. Here, we report the molecular structure of human MCM10 as determined by electron microscopy and single-particle analysis. The MCM10 molecule is a ring-shaped hexamer with large central and smaller lateral channels and a system of inner chambers. This structure, together with biochemical data, suggests that this important protein uses its architecture to provide a docking module for assembly of the molecular machinery required for eukaryotic DNA replication.
Original language | English (US) |
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Pages (from-to) | 925-930 |
Number of pages | 6 |
Journal | EMBO reports |
Volume | 8 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2007 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics