Hexameric ring structure of human MCM10 DNA replication factor

  • Andrei L. Okorokov
  • , Alastair Waugh
  • , Julie Hodgkinson
  • , Andal Murthy
  • , Hye Kyung Hong
  • , Elisabetta Leo
  • , Michael B. Sherman
  • , Kai Stoeber
  • , Elena V. Orlova
  • , Gareth H. Williams

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)925-930
Number of pages6
JournalEMBO reports
Volume8
Issue number10
DOIs
StatePublished - Oct 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

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