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- PDB-6zz6: Cryo-EM structure of S.cerevisiae cohesin-Scc2-DNA complex -

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Basic information

Entry
Database: PDB / ID: 6zz6
TitleCryo-EM structure of S.cerevisiae cohesin-Scc2-DNA complex
Components
  • (DNA (34-MER)) x 2
  • (Sister chromatid cohesion protein ...) x 2
  • (Structural maintenance of chromosomes protein ...) x 2
KeywordsCELL CYCLE / SMC / cohesin / DNA
Function / homology
Function and homology information


SMC loading complex / Scc2-Scc4 cohesin loading complex / mitotic cohesin loading / 2-micrometer circle DNA / Establishment of Sister Chromatid Cohesion / Resolution of Sister Chromatid Cohesion / cohesin loader activity / tRNA gene clustering / meiotic cohesin complex / establishment of meiotic sister chromatid cohesion ...SMC loading complex / Scc2-Scc4 cohesin loading complex / mitotic cohesin loading / 2-micrometer circle DNA / Establishment of Sister Chromatid Cohesion / Resolution of Sister Chromatid Cohesion / cohesin loader activity / tRNA gene clustering / meiotic cohesin complex / establishment of meiotic sister chromatid cohesion / mitotic cohesin complex / DNA secondary structure binding / cohesin complex / rDNA chromatin condensation / establishment of protein localization to chromatin / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / synaptonemal complex assembly / SUMOylation of DNA damage response and repair proteins / meiotic sister chromatid cohesion / replication-born double-strand break repair via sister chromatid exchange / establishment of mitotic sister chromatid cohesion / reciprocal meiotic recombination / mitotic chromosome condensation / sister chromatid cohesion / mitotic sister chromatid cohesion / protein acetylation / minor groove of adenine-thymine-rich DNA binding / mitotic sister chromatid segregation / chromosome, centromeric region / protein localization to chromatin / condensed nuclear chromosome / double-strand break repair / double-stranded DNA binding / regulation of gene expression / sequence-specific DNA binding / cell division / apoptotic process / DNA damage response / chromatin binding / chromatin / protein kinase binding / ATP hydrolysis activity / mitochondrion / DNA binding / ATP binding / identical protein binding / nucleus / cytosol
Similarity search - Function
Sister chromatid cohesion C-terminal domain / HEAT repeat associated with sister chromatid cohesion protein / Scc2/Nipped-B family / Sister chromatid cohesion C-terminus / HEAT repeat associated with sister chromatid cohesion / Smc1, ATP-binding cassette domain / Rad21/Rec8-like protein, C-terminal, eukaryotic / Rad21/Rec8-like protein, N-terminal / Rad21/Rec8-like protein / Structural maintenance of chromosomes 3, ABC domain, eukaryotic ...Sister chromatid cohesion C-terminal domain / HEAT repeat associated with sister chromatid cohesion protein / Scc2/Nipped-B family / Sister chromatid cohesion C-terminus / HEAT repeat associated with sister chromatid cohesion / Smc1, ATP-binding cassette domain / Rad21/Rec8-like protein, C-terminal, eukaryotic / Rad21/Rec8-like protein, N-terminal / Rad21/Rec8-like protein / Structural maintenance of chromosomes 3, ABC domain, eukaryotic / Conserved region of Rad21 / Rec8 like protein / N terminus of Rad21 / Rec8 like protein / ScpA-like, C-terminal / Structural maintenance of chromosomes protein / SMCs flexible hinge / SMCs flexible hinge superfamily / SMC proteins Flexible Hinge Domain / SMC proteins Flexible Hinge Domain / RecF/RecN/SMC, N-terminal / RecF/RecN/SMC N terminal domain / Armadillo-type fold / Winged helix DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / DNA / DNA (> 10) / Structural maintenance of chromosomes protein 1 / Structural maintenance of chromosomes protein 3 / Sister chromatid cohesion protein 2 / Sister chromatid cohesion protein 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
synthetic construct (others)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsLee, B.-G. / Gonzalez Llamazares, A. / Collier, J. / Nasmyth, K.A. / Lowe, J.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust202754/Z/16/Z United Kingdom
Medical Research Council (MRC, United Kingdom)U105184326 United Kingdom
CitationJournal: Elife / Year: 2020
Title: Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3.
Authors: James E Collier / Byung-Gil Lee / Maurici Brunet Roig / Stanislav Yatskevich / Naomi J Petela / Jean Metson / Menelaos Voulgaris / Andres Gonzalez Llamazares / Jan Löwe / Kim A Nasmyth /
Abstract: In addition to extruding DNA loops, cohesin entraps within its SMC-kleisin ring (S-K) individual DNAs during G1 and sister DNAs during S-phase. All three activities require related hook-shaped ...In addition to extruding DNA loops, cohesin entraps within its SMC-kleisin ring (S-K) individual DNAs during G1 and sister DNAs during S-phase. All three activities require related hook-shaped proteins called Scc2 and Scc3. Using thiol-specific crosslinking we provide rigorous proof of entrapment activity in vitro. Scc2 alone promotes entrapment of DNAs in the E-S and E-K compartments, between ATP-bound engaged heads and the SMC hinge and associated kleisin, respectively. This does not require ATP hydrolysis nor is it accompanied by entrapment within S-K rings, which is a slower process requiring Scc3. Cryo-EM reveals that DNAs transported into E-S/E-K compartments are 'clamped' in a sub-compartment created by Scc2's association with engaged heads whose coiled coils are folded around their elbow. We suggest that clamping may be a recurrent feature of cohesin complexes active in loop extrusion and that this conformation precedes the S-K entrapment required for sister chromatid cohesion.
History
DepositionAug 4, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 30, 2020Provider: repository / Type: Initial release

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Structure visualization

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Assembly

Deposited unit
A: Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1
B: Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3
C: Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1
D: Sister chromatid cohesion protein 2
F: DNA (34-MER)
G: DNA (34-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)291,54810
Polymers290,4856
Non-polymers1,0634
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Structural maintenance of chromosomes protein ... , 2 types, 2 molecules AB

#1: Protein Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1 / DA-box protein SMC1


Mass: 40854.500 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: 2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044- ...Details: 2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224,2-71, 87-195, 1044-1224
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: SMC1, CHL10, YFL008W / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P32908
#2: Protein Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3 / DA-box protein SMC3


Mass: 48295.016 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: 0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, ...Details: 0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222,0-224, 997-1071,1104-1222
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: SMC3, YJL074C, J1049 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P47037

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Sister chromatid cohesion protein ... , 2 types, 2 molecules CD

#3: Protein Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1


Mass: 9123.593 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: 67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502- ...Details: 67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555,67-103, 502-510, 519-555
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: MCD1, PDS3, RHC21, SCC1, YDL003W, YD8119.04 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q12158
#4: Protein Sister chromatid cohesion protein 2


Mass: 171310.625 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: SCC2, YDR180W, YD9395.14 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q04002

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DNA chain , 2 types, 2 molecules FG

#5: DNA chain DNA (34-MER)


Mass: 10604.072 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#6: DNA chain DNA (34-MER)


Mass: 10297.598 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 2 types, 4 molecules

#7: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSource
1Complex of cohesin, Scc2, ATP and DNACOMPLEX#1-#60RECOMBINANT
2Complex of cohesin and Scc2COMPLEX#1-#41RECOMBINANT
3double strand DNACOMPLEX#5-#61RECOMBINANT
Molecular weightValue: 0.485 MDa / Experimental value: YES
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
22Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)559292
33synthetic construct (others)32630
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
22Spodoptera frugiperda (fall armyworm)7108
33synthetic construct (others)32630
Buffer solutionpH: 7.5
SpecimenConc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: UltrAuFoil
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 100 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 81000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 1500 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 55 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: EPU / Category: image acquisition
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 588164 / Symmetry type: POINT

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