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TitleHexameric ring structure of human MCM10 DNA replication factor.
Journal, issue, pagesEMBO Rep, Vol. 8, Issue 10, Page 925-930, Year 2007
Publish dateSep 7, 2007
AuthorsAndrei L Okorokov / Alastair Waugh / Julie Hodgkinson / Andal Murthy / Hye Kyung Hong / Elisabetta Leo / Michael B Sherman / Kai Stoeber / Elena V Orlova / Gareth H Williams /
PubMed AbstractThe 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- ...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.
External linksEMBO Rep / PubMed:17823614 / PubMed Central
MethodsEM (single particle)
Resolution16.0 Å
Structure data

EMDB-1254:
Hexameric ring structure of human MCM10 DNA replication factor.
Method: EM (single particle) / Resolution: 16.0 Å

Source
  • Homo sapiens (human)

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