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Structure paper

TitleCdt1 stabilizes an open MCM ring for helicase loading.
Journal, issue, pagesNat Commun, Vol. 8, Page 15720, Year 2017
Publish dateJun 23, 2017
AuthorsJordi Frigola / Jun He / Kerstin Kinkelin / Valerie E Pye / Ludovic Renault / Max E Douglas / Dirk Remus / Peter Cherepanov / Alessandro Costa / John F X Diffley /
PubMed AbstractORC, Cdc6 and Cdt1 act together to load hexameric MCM, the motor of the eukaryotic replicative helicase, into double hexamers at replication origins. Here we show that Cdt1 interacts with MCM ...ORC, Cdc6 and Cdt1 act together to load hexameric MCM, the motor of the eukaryotic replicative helicase, into double hexamers at replication origins. Here we show that Cdt1 interacts with MCM subunits Mcm2, 4 and 6, which both destabilizes the Mcm2-5 interface and inhibits MCM ATPase activity. Using X-ray crystallography, we show that Cdt1 contains two winged-helix domains in the C-terminal half of the protein and a catalytically inactive dioxygenase-related N-terminal domain, which is important for MCM loading, but not for subsequent replication. We used these structures together with single-particle electron microscopy to generate three-dimensional models of MCM complexes. These show that Cdt1 stabilizes MCM in a left-handed spiral open at the Mcm2-5 gate. We propose that Cdt1 acts as a brace, holding MCM open for DNA entry and bound to ATP until ORC-Cdc6 triggers ATP hydrolysis by MCM, promoting both Cdt1 ejection and MCM ring closure.
External linksNat Commun / PubMed:28643783 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.8 - 20.4 Å
Structure data

EMDB-3679:
Full-length complex of S.cerevisiae Cdt1-MCM in apo state.
Method: EM (single particle) / Resolution: 20.4 Å

EMDB-3680:
Full-length complex of S.cerevisiae Cdt1-MCM in ATPgS-bound state.
Method: EM (single particle) / Resolution: 20.4 Å

EMDB-3681:
Full-length complex of S.cerevisiae MCM in ATPgS-bound state.
Method: EM (single particle) / Resolution: 20.4 Å

PDB-5me9:
Crystal structure of yeast Cdt1 (N terminal and middle domain), form 1.
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-5mea:
Crystal structure of yeast Cdt1 (N terminal and middle domain), form 2.
Method: X-RAY DIFFRACTION / Resolution: 2.152 Å

PDB-5meb:
Crystal structure of yeast Cdt1 C-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5mec:
Crystal structure of yeast Cdt1 middle domain (residues 294-433)
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCELL CYCLE / Cdt1 / MCM / winged helix / yeast / DNA replication

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