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EMBO reports 8, 10, 925–930 (2007)
doi:10.1038/sj.embor.7401064
AOP Published online: 7 September 2007
Hexameric ring structure of human MCM10 DNA replication factor
Andrei L Okorokov1, 2, Alastair Waugh2, Julie Hodgkinson3, Andal Murthy2, Hye Kyung Hong1, 2, Elisabetta Leo2, Michael B Sherman4, Kai Stoeber1, 2, Elena V Orlova3 & Gareth H Williams1, 2
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1 Department of Pathology, University College London, London WC1E 6JJ, UK
2 Wolfson Institute for Biomedical Research, University College London, Cruciform Building, Gower Street, London WC1E 6BT, UK
3 School of Crystallography, Birkbeck College, Bloomsbury, Malet Street, London WC1E 7HX, UK
4 Department of Biochemistry & Molecular Biology, 1.224 Medical Research Building, University of Texas Medical Branch, Galveston, Texas 77555-1055, USA
To whom correspondence should be addressed
Andrei L Okorokov Tel: +44 20 7679 0959; Fax: +44 20 7388 4408; E-mail: a.okorokov@ucl.ac.uk
Elena V Orlova Tel: +44 (0) 20 7631 6845; Fax: +44 (0) 20 7631 6803; E-mail: e.orlova@mail.cryst.bbk.ac.uk
Received 28 March 2007; Accepted 2 August 2007; Published online 7 September 2007.
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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.
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