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- PDB-8uru: Spo11 core complex with hairpin DNA -

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Basic information

Entry
Database: PDB / ID: 8uru
TitleSpo11 core complex with hairpin DNA
Components
  • (Meiotic recombination protein ...) x 2
  • Antiviral protein SKI8
  • Hairpin DNA
  • Meiosis-specific protein SPO11
KeywordsDNA BINDING PROTEIN / Spo11 / Rec102 / Rec104 / Ski8 / DNA binding / Cross over.
Function / homology
Function and homology information


meiotic DNA double-strand break processing / mRNA decay by 3' to 5' exoribonuclease / protein-DNA complex assembly / meiotic DNA double-strand break formation / Ski complex / nuclear-transcribed mRNA catabolic process, non-stop decay / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / DNA end binding / synaptonemal complex assembly / homologous chromosome pairing at meiosis ...meiotic DNA double-strand break processing / mRNA decay by 3' to 5' exoribonuclease / protein-DNA complex assembly / meiotic DNA double-strand break formation / Ski complex / nuclear-transcribed mRNA catabolic process, non-stop decay / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / DNA end binding / synaptonemal complex assembly / homologous chromosome pairing at meiosis / meiosis I / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / reciprocal meiotic recombination / DNA topoisomerase (ATP-hydrolysing) / sporulation resulting in formation of a cellular spore / nuclear chromosome / mRNA catabolic process / nuclear-transcribed mRNA catabolic process / condensed nuclear chromosome / site of double-strand break / protein-containing complex assembly / defense response to virus / chromatin binding / DNA binding / nucleoplasm / ATP binding / metal ion binding / nucleus / cytoplasm
Similarity search - Function
Meiotic recombination protein Rec104 / : / Meiotic recombination protein REC104 / REC102 protein / Spo11/DNA topoisomerase VI subunit A / Spo11/DNA topoisomerase VI, subunit A, N-terminal / Topoisomerase 6 subunit A/Spo11, TOPRIM domain / Spo11/DNA topoisomerase VI subunit A superfamily / Type IIB DNA topoisomerase / Topoisomerase 6 subunit A/Spo11, Toprim domain ...Meiotic recombination protein Rec104 / : / Meiotic recombination protein REC104 / REC102 protein / Spo11/DNA topoisomerase VI subunit A / Spo11/DNA topoisomerase VI, subunit A, N-terminal / Topoisomerase 6 subunit A/Spo11, TOPRIM domain / Spo11/DNA topoisomerase VI subunit A superfamily / Type IIB DNA topoisomerase / Topoisomerase 6 subunit A/Spo11, Toprim domain / Topoisomerase (Topo) IIB-type catalytic domain profile. / : / WD domain, G-beta repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / Winged helix-like DNA-binding domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
DNA / DNA (> 10) / Meiosis-specific protein SPO11 / Meiotic recombination protein REC104 / Meiotic recombination protein REC102 / Antiviral protein SKI8
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288C (yeast)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsYu, Y. / Patel, D.J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)R01 HD110120 United States
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: Cryo-EM structures of the Spo11 core complex bound to DNA.
Authors: You Yu / Juncheng Wang / Kaixian Liu / Zhi Zheng / Meret Arter / Corentin Claeys Bouuaert / Stephen Pu / Dinshaw J Patel / Scott Keeney /
Abstract: DNA double-strand breaks that initiate meiotic recombination are formed by the topoisomerase-relative enzyme Spo11, supported by conserved auxiliary factors. Because high-resolution structural data ...DNA double-strand breaks that initiate meiotic recombination are formed by the topoisomerase-relative enzyme Spo11, supported by conserved auxiliary factors. Because high-resolution structural data have not been available, many questions remain about the architecture of Spo11 and its partners and how they engage with DNA. We report cryo-electron microscopy structures at up to 3.3-Å resolution of DNA-bound core complexes of Saccharomyces cerevisiae Spo11 with Rec102, Rec104 and Ski8. In these structures, monomeric core complexes make extensive contacts with the DNA backbone and with the recessed 3'-OH and first 5' overhanging nucleotide, establishing the molecular determinants of DNA end-binding specificity and providing insight into DNA cleavage preferences in vivo. The structures of individual subunits and their interfaces, supported by functional data in yeast, provide insight into the role of metal ions in DNA binding and uncover unexpected structural variation in homologs of the Top6BL component of the core complex.
History
DepositionOct 26, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 26, 2024Provider: repository / Type: Initial release
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Revision 1.1Oct 9, 2024Group: Data collection / Database references / Structure summary
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Meiosis-specific protein SPO11
B: Meiotic recombination protein REC102
C: Antiviral protein SKI8
F: Meiotic recombination protein REC104
D: Hairpin DNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,2446
Polymers160,2205
Non-polymers241
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 2 types, 2 molecules AC

#1: Protein Meiosis-specific protein SPO11


Mass: 50020.109 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Gene: SPO11 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P23179
#3: Protein Antiviral protein SKI8


Mass: 44313.555 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Gene: SKI8 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q02793

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Meiotic recombination protein ... , 2 types, 2 molecules BF

#2: Protein Meiotic recombination protein REC102


Mass: 30283.771 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Gene: REC102 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q02721
#4: Protein Meiotic recombination protein REC104


Mass: 20821.182 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Gene: REC104 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P33323

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DNA chain / Non-polymers , 2 types, 2 molecules D

#5: DNA chain Hairpin DNA


Mass: 14781.522 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Saccharomyces cerevisiae S288C (yeast)
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY
Has protein modificationN

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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

ComponentName: Spo11 core complex bound to gapped DNA / Type: COMPLEX / Entity ID: #1-#5 / Source: RECOMBINANT
Molecular weightValue: 0.14 MDa / Experimental value: NO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.4
Details: 25 mM HEPES, pH 7.4, 300 mM NaCl, 5 mM EDTA, 2 mM DTT
SpecimenConc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 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 FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm
Image recordingAverage exposure time: 3 sec. / Electron dose: 53 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameCategory
2SerialEMimage acquisition
8PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 128787 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0039172
ELECTRON MICROSCOPYf_angle_d0.84812571
ELECTRON MICROSCOPYf_dihedral_angle_d19.5231472
ELECTRON MICROSCOPYf_chiral_restr0.0431434
ELECTRON MICROSCOPYf_plane_restr0.0071429

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