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- PDB-9hjt: Structure of Zincore (SEPHS1:QRICH1) binding to ZFP91 on DNA -

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Basic information

Entry
Database: PDB / ID: 9hjt
TitleStructure of Zincore (SEPHS1:QRICH1) binding to ZFP91 on DNA
Components
  • (DNA (31-MER)) x 2
  • E3 ubiquitin-protein ligase ZFP91
  • Selenide, water dikinase 1
  • Transcriptional regulator QRICH1
KeywordsSTRUCTURAL PROTEIN / Zincore Complex / Transcriptional regulator complex / SEPHS1 / Selenide / water dikinase 1 / selenophosphate synthetase 1 / QRICH1 / Zinc finger protein / ZFP91 / Transcription factor
Function / homology
Function and homology information


selenide, water dikinase / selenide, water dikinase activity / integrated stress response signaling / selenocysteine biosynthetic process / PERK-mediated unfolded protein response / activation of NF-kappaB-inducing kinase activity / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / protein K63-linked ubiquitination / endoplasmic reticulum unfolded protein response / response to endoplasmic reticulum stress ...selenide, water dikinase / selenide, water dikinase activity / integrated stress response signaling / selenocysteine biosynthetic process / PERK-mediated unfolded protein response / activation of NF-kappaB-inducing kinase activity / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / protein K63-linked ubiquitination / endoplasmic reticulum unfolded protein response / response to endoplasmic reticulum stress / protein modification process / RING-type E3 ubiquitin transferase / ubiquitin-protein transferase activity / nuclear membrane / positive regulation of apoptotic process / protein heterodimerization activity / regulation of transcription by RNA polymerase II / GTP binding / positive regulation of DNA-templated transcription / nucleolus / protein homodimerization activity / DNA binding / zinc ion binding / nucleoplasm / ATP binding / metal ion binding / identical protein binding / nucleus / plasma membrane / cytoplasm
Similarity search - Function
Protein of unknown function DUF3504 / Domain of unknown function (DUF3504) / : / Selenophosphate synthetase / : / PurM-like, N-terminal domain / AIR synthase related protein, N-terminal domain / PurM-like, C-terminal domain / PurM-like, C-terminal domain superfamily / PurM-like, N-terminal domain superfamily ...Protein of unknown function DUF3504 / Domain of unknown function (DUF3504) / : / Selenophosphate synthetase / : / PurM-like, N-terminal domain / AIR synthase related protein, N-terminal domain / PurM-like, C-terminal domain / PurM-like, C-terminal domain superfamily / PurM-like, N-terminal domain superfamily / AIR synthase related protein, C-terminal domain / Zinc finger, C2H2 type / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type
Similarity search - Domain/homology
DNA / DNA (> 10) / Selenide, water dikinase 1 / Transcriptional regulator QRICH1 / E3 ubiquitin-protein ligase ZFP91
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.26 Å
AuthorsBorza, R. / Perrakis, A.
Funding support Netherlands, 1items
OrganizationGrant numberCountry
Oncode Institute Netherlands
CitationJournal: Science / Year: 2025
Title: Zincore, an atypical coregulator, binds zinc finger transcription factors to control gene expression
Authors: Bianchi, D. / Borza, R. / De Zan, E. / Huelsz-Prince, G. / Gregoricchio, S. / Dekker, M. / Fish, A. / Mazouzi, A. / Kroese, L. / Linder, S. / Hernandez Quiles, M. / Vermeulen, M. / Celie, P. ...Authors: Bianchi, D. / Borza, R. / De Zan, E. / Huelsz-Prince, G. / Gregoricchio, S. / Dekker, M. / Fish, A. / Mazouzi, A. / Kroese, L. / Linder, S. / Hernandez Quiles, M. / Vermeulen, M. / Celie, P. / Krimpenfort, P. / Song, J. / Zwart, W. / Wessels, L. / Nijman, S. / Perrakis, A. / Brummelkamp, T.
History
DepositionDec 2, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 9, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase ZFP91
F: Selenide, water dikinase 1
G: Selenide, water dikinase 1
H: Transcriptional regulator QRICH1
I: Transcriptional regulator QRICH1
K: DNA (31-MER)
L: DNA (31-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)341,87612
Polymers341,5497
Non-polymers3275
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Protein , 3 types, 5 molecules AFGHI

#1: Protein E3 ubiquitin-protein ligase ZFP91 / RING-type E3 ubiquitin transferase ZFP91 / Zinc finger protein 757 / Zinc finger protein 91 homolog / Zfp-91


Mass: 63557.219 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ZFP91, ZNF757, FKSG11 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q96JP5, RING-type E3 ubiquitin transferase
#2: Protein Selenide, water dikinase 1 / Selenium donor protein 1 / Selenophosphate synthase 1


Mass: 42953.461 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEPHS1, SELD, SPS, SPS1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P49903, selenide, water dikinase
#3: Protein Transcriptional regulator QRICH1 / Glutamine-rich protein 1


Mass: 86507.156 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: QRICH1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q2TAL8

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DNA chain , 2 types, 2 molecules KL

#4: DNA chain DNA (31-MER)


Mass: 9314.979 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#5: DNA chain DNA (31-MER)


Mass: 9755.242 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)

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Non-polymers , 1 types, 5 molecules

#6: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn

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Details

Has ligand of interestN
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: Zincore / Type: COMPLEX / Entity ID: #1, #3-#5, #2 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 7542

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
2Topazparticle selection
3EPUimage acquisition
5cryoSPARCCTF correction
8UCSF ChimeraXmodel fitting
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
13cryoSPARC3D reconstruction
14PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionDetails: Multiple particle selections
3D reconstructionResolution: 3.26 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 42621 / Symmetry type: POINT
Atomic model buildingSpace: REAL
Atomic model buildingSource name: AlphaFold / Type: in silico model
RefinementHighest resolution: 3.26 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00313731
ELECTRON MICROSCOPYf_angle_d0.50218866
ELECTRON MICROSCOPYf_dihedral_angle_d17.2852251
ELECTRON MICROSCOPYf_chiral_restr0.0392103
ELECTRON MICROSCOPYf_plane_restr0.0032216

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