Structure of the eukaryotic replicative CMG helicase suggests a pumpjack motion for translocation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-03

AUTHORS

Zuanning Yuan, Lin Bai, Jingchuan Sun, Roxana Georgescu, Jun Liu, Michael E O'Donnell, Huilin Li

ABSTRACT

The CMG helicase is composed of Cdc45, Mcm2-7 and GINS. Here we report the structure of the Saccharomyces cerevisiae CMG, determined by cryo-EM at a resolution of 3.7-4.8 Å. The structure reveals that GINS and Cdc45 scaffold the N tier of the helicase while enabling motion of the AAA+ C tier. CMG exists in two alternating conformations, compact and extended, thus suggesting that the helicase moves like an inchworm. The N-terminal regions of Mcm2-7, braced by Cdc45-GINS, form a rigid platform upon which the AAA+ C domains make longitudinal motions, nodding up and down like an oil-rig pumpjack attached to a stable platform. The Mcm ring is remodeled in CMG relative to the inactive Mcm2-7 double hexamer. The Mcm5 winged-helix domain is inserted into the central channel, thus blocking entry of double-stranded DNA and supporting a steric-exclusion DNA-unwinding model. More... »

PAGES

217-224

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb.3170

    DOI

    http://dx.doi.org/10.1038/nsmb.3170

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1053369012

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26854665


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