| Literature DB >> 17823614 |
Andrei L Okorokov1, Alastair Waugh, Julie Hodgkinson, Andal Murthy, Hye Kyung Hong, Elisabetta Leo, Michael B Sherman, Kai Stoeber, Elena V Orlova, Gareth H Williams.
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.Entities:
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Year: 2007 PMID: 17823614 PMCID: PMC2002553 DOI: 10.1038/sj.embor.7401064
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807