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TitleCryo-electron microscopy reveals a novel DNA-binding site on the MCM helicase.
Journal, issue, pagesEMBO J, Vol. 27, Issue 16, Page 2250-2258, Year 2008
Publish dateAug 20, 2008
AuthorsAlessandro Costa / Gijs van Duinen / Barbara Medagli / James Chong / Nozomi Sakakibara / Zvi Kelman / Satish K Nair / Ardan Patwardhan / Silvia Onesti /
PubMed AbstractThe eukaryotic MCM2-7 complex is recruited at origins of replication during the G1 phase and acts as the main helicase at the replication fork during the S phase of the cell cycle. To characterize ...The eukaryotic MCM2-7 complex is recruited at origins of replication during the G1 phase and acts as the main helicase at the replication fork during the S phase of the cell cycle. To characterize the interplay between the MCM helicase and DNA prior to the melting of the double helix, we determined the structure of an archaeal MCM orthologue bound to a 5.6-kb double-stranded DNA segment, using cryo-electron microscopy. DNA wraps around the N-terminal face of a single hexameric ring. This interaction requires a conformational change within the outer belt of the MCM N-terminal domain, exposing a previously unrecognized helix-turn-helix DNA-binding motif. Our findings provide novel insights into the role of the MCM complex during the initiation step of DNA replication.
External linksEMBO J / PubMed:18650940 / PubMed Central
MethodsEM (single particle)
Resolution19.0 Å
Structure data

EMDB-1526:
Single particle reconstruction of Methanothermobacter thermautotrophicus MCM protein bound to a 5,600bp dsDNA fragment.
Method: EM (single particle) / Resolution: 19.0 Å

Source
  • synthetic construct (others)
  • Methanothermobacter thermautotrophicus str. Delta H (archaea)

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