Hexameric ring structure of human MCM10 DNA replication factor.
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.
Okorokov
Andrei L
AL
Department of Pathology, University College London, London WC1E 6JJ, UK.
Waugh
Alastair
A
Hodgkinson
Julie
J
Murthy
Andal
A
Hong
Hye Kyung
HK
Leo
Elisabetta
E
Sherman
Michael B
MB
Stoeber
Kai
K
Orlova
Elena V
EV
Williams
Gareth H
GH
D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D004261:DNA Replication; D019281:Dimerization; D006801:Humans; D008854:Microscopy, Electron; D064110:Minichromosome Maintenance Proteins; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure