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Yorodumi- PDB-11ss: Cryo-EM structure of DNA polymerase Zeta with RNA:DNA hybrid and ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 11ss | |||||||||
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| Title | Cryo-EM structure of DNA polymerase Zeta with RNA:DNA hybrid and incoming dNTP | |||||||||
Components |
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Keywords | DNA BINDING PROTEIN/DNA/RNA / Protein complex / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA-RNA complex | |||||||||
| Function / homology | Function and homology informationTranslesion synthesis by REV1 / delta DNA polymerase complex / DNA amplification / deoxycytidyl transferase activity / H3-H4 histone complex chaperone activity / zeta DNA polymerase complex / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / RNA-templated DNA biosynthetic process / DNA replication, removal of RNA primer ...Translesion synthesis by REV1 / delta DNA polymerase complex / DNA amplification / deoxycytidyl transferase activity / H3-H4 histone complex chaperone activity / zeta DNA polymerase complex / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / RNA-templated DNA biosynthetic process / DNA replication, removal of RNA primer / lagging strand elongation / DNA damage tolerance / error-free translesion synthesis / double-strand break repair via break-induced replication / DNA metabolic process / DNA strand elongation involved in DNA replication / leading strand elongation / error-prone translesion synthesis / mismatch repair / translesion synthesis / replication fork / double-strand break repair via homologous recombination / nucleotide-excision repair / base-excision repair / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / site of double-strand break / DNA-directed DNA polymerase / damaged DNA binding / DNA-directed DNA polymerase activity / molecular adaptor activity / nucleotide binding / DNA repair / chromatin / mitochondrion / DNA binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() synthetic construct (others) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å | |||||||||
Authors | Malik, R. / Aggarwal, A.K. | |||||||||
| Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Molecular basis of DNA polymerase zeta's reverse transcriptase activity Authors: Malik, R. / Johnson, R.E. / Prakash, L. / Prakash, S. / Aggarwal, A.K. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 11ss.cif.gz | 536.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb11ss.ent.gz | 395.7 KB | Display | PDB format |
| PDBx/mmJSON format | 11ss.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1s/11ss ftp://data.pdbj.org/pub/pdb/validation_reports/1s/11ss | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 76020MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-DNA polymerase zeta ... , 2 types, 3 molecules ADE
| #1: Protein | Mass: 177068.516 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: REV3, PSO1, YPL167C, P2535 / Production host: ![]() |
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| #2: Protein | Mass: 28791.654 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: REV7, YIL139C / Production host: ![]() |
-DNA polymerase delta ... , 2 types, 2 molecules GF
| #3: Protein | Mass: 40377.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: POL32, YJR043C, J1626 / Production host: ![]() |
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| #6: Protein | Mass: 55987.352 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: POL31, HUS2, HYS2, SDP5, YJR006W, J1427, YJR83.7 / Production host: ![]() |
-Protein / DNA chain / RNA chain , 3 types, 3 molecules BPX
| #4: Protein | Mass: 112384.219 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: REV1, YOR346W, O6339 / Production host: ![]() References: UniProt: P12689, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases |
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| #5: DNA chain | Mass: 6132.991 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
| #7: RNA chain | Mass: 7984.772 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 4 types, 10 molecules 






| #8: Chemical | ChemComp-CA / |
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| #9: Chemical | ChemComp-DCP / |
| #10: Chemical | ChemComp-SF4 / |
| #11: Water | ChemComp-HOH / |
-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Source (natural) |
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| Source (recombinant) | Organism: ![]() | ||||||||||||||||||||||||
| Buffer solution | pH: 6.5 | ||||||||||||||||||||||||
| Specimen | Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| EM embedding | Material: VITREOUS ICE | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 54.24 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 544413 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.03 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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