Journal: Nat Struct Mol Biol / Year: 2011 Title: The structural basis for MCM2-7 helicase activation by GINS and Cdc45. Authors: Alessandro Costa / Ivar Ilves / Nele Tamberg / Tatjana Petojevic / Eva Nogales / Michael R Botchan / James M Berger / Abstract: Two central steps for initiating eukaryotic DNA replication involve loading of the Mcm2-7 helicase onto double-stranded DNA and its activation by GINS-Cdc45. To better understand these events, we ...Two central steps for initiating eukaryotic DNA replication involve loading of the Mcm2-7 helicase onto double-stranded DNA and its activation by GINS-Cdc45. To better understand these events, we determined the structures of Mcm2-7 and the CMG complex by using single-particle electron microscopy. Mcm2-7 adopts two conformations--a lock-washer-shaped spiral state and a planar, gapped-ring form--in which Mcm2 and Mcm5 flank a breach in the helicase perimeter. GINS and Cdc45 bridge this gap, forming a topologically closed assembly with a large interior channel; nucleotide binding further seals off the discontinuity between Mcm2 and Mcm5, partitioning the channel into two smaller pores. Together, our data help explain how GINS and Cdc45 activate Mcm2-7, indicate that Mcm2-7 loading may be assisted by a natural predisposition of the hexamer to form open rings, and suggest a mechanism by which the CMG complex assists DNA strand separation.
History
Deposition
Nov 28, 2010
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Header (metadata) release
Dec 9, 2010
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Map release
Apr 8, 2011
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Update
Apr 8, 2011
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Current status
Apr 8, 2011
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Download / File: emd_1833.map.gz / Format: CCP4 / Size: 1001 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation
This is the volume file of the apo CMG complex
Voxel size
X=Y=Z: 5.7 Å
Density
Contour Level
By AUTHOR: 0.377 / Movie #1: 0.377
Minimum - Maximum
-0.169495 - 2.34794
Average (Standard dev.)
-0.0000372498 (±0.146242)
Symmetry
Space group: 1
Details
EMDB XML:
Map geometry
Axis order
X
Y
Z
Origin
-32
-32
-32
Dimensions
64
64
64
Spacing
64
64
64
Cell
A=B=C: 364.8 Å α=β=γ: 90 °
CCP4 map header:
mode
Image stored as Reals
Å/pix. X/Y/Z
5.7
5.7
5.7
M x/y/z
64
64
64
origin x/y/z
0.000
0.000
0.000
length x/y/z
364.800
364.800
364.800
α/β/γ
90.000
90.000
90.000
start NX/NY/NZ
-30
-24
-70
NX/NY/NZ
61
49
141
MAP C/R/S
1
2
3
start NC/NR/NS
-32
-32
-32
NC/NR/NS
64
64
64
D min/max/mean
-0.169
2.348
-0.000
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Supplemental data
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Sample components
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Entire : Drosophila melanogaster CMG complex - APO
Entire
Name: Drosophila melanogaster CMG complex - APO
Components
Sample: Drosophila melanogaster CMG complex - APO
Protein or peptide: Mcm2
Protein or peptide: Mcm3
Protein or peptide: Mcm4
Protein or peptide: Mcm5
Protein or peptide: Mcm6
Protein or peptide: Mcm7
Protein or peptide: Psf1
Protein or peptide: Psf2
Protein or peptide: Psf3
Protein or peptide: Sld5
Protein or peptide: Cdc45
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Supramolecule #1000: Drosophila melanogaster CMG complex - APO
Supramolecule
Name: Drosophila melanogaster CMG complex - APO / type: sample / ID: 1000 / Details: The sample was monodisperse Oligomeric state: One Mcm2-7 heterohexamer binds to one GINS heterotetramer and a Cdc45 monomer Number unique components: 11
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