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- EMDB-52125: Cryo-EM structure of human CDADC1 inactive mutant (E400A): trimer... -

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Basic information

Entry
Database: EMDB / ID: EMD-52125
TitleCryo-EM structure of human CDADC1 inactive mutant (E400A): trimer in the presence of 5mdCTP in solution (not bound)
Map data
Sample
  • Complex: Human CDADC1 trimer without a ligand (solution with 5mdCTP)
    • Protein or peptide: Human CDADC1
KeywordsHuman dCTP deaminase / trimer / Zinc-dependent / Nucleotide metabolism / HYDROLASE
Function / homology
Function and homology information


dCMP deaminase activity / cytidine deaminase / : / DNA cytosine deamination / importin-alpha family protein binding / cytidine deaminase activity / protein homodimerization activity / zinc ion binding / nucleus / cytoplasm
Similarity search - Function
Deoxycytidylate deaminase domain / Deoxycytidylate deaminase-related / Cytidine and deoxycytidylate deaminase zinc-binding region / APOBEC/CMP deaminase, zinc-binding / Cytidine and deoxycytidylate deaminases zinc-binding region signature. / Cytidine and deoxycytidylate deaminase domain / Cytidine and deoxycytidylate deaminases domain profile. / Cytidine deaminase-like
Similarity search - Domain/homology
Cytidine and dCMP deaminase domain-containing protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.81 Å
AuthorsSlyvka A / Rathore I / Yang R / Kanai T / Lountos G / Wang Z / Skowronek K / Czarnocki-Cieciura M / Wlodawer A / Bochtler M
Funding support Poland, United States, 4 items
OrganizationGrant numberCountry
Foundation for Polish SciencePOIR.04.04.00-00-5D81/17-00 Poland
Ministry of Science and Higher Education (Poland)PPI/APM/2018/1/00034 Poland
National Institutes of Health/National Cancer Institute (NIH/NCI)NIH Intramural Research Program United States
National Institutes of Health/National Cancer Institute (NIH/NCI)75N91019D00024 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2025
Title: Activity and structure of human (d)CTP deaminase CDADC1.
Authors: Anton Slyvka / Ishan Rathore / Renbin Yang / Olga Gewartowska / Tapan Kanai / George T Lountos / Krzysztof Skowronek / Mariusz Czarnocki-Cieciura / Alexander Wlodawer / Matthias Bochtler /
Abstract: Vertebrates have evolved an understudied protein termed CDADC1 (NYD-SP15) that contains an inactive N-terminal and active C-terminal DCTD-like domain. Here, we show that human CDADC1 is a (d)CTP- ...Vertebrates have evolved an understudied protein termed CDADC1 (NYD-SP15) that contains an inactive N-terminal and active C-terminal DCTD-like domain. Here, we show that human CDADC1 is a (d)CTP-specific deaminase, with a roughly 2-fold in vitro preference for dCTP over CTP. We determined high-resolution cryo-EM structures of CDADC1 in the absence of substrate and in complex with dCTP and 5-methyl-dCTP. The structures show that CDADC1 forms trimers and dimers of trimers in solution. The (d)CTP substrate is selected by a narrow pocket for the cytosine base and multiple lysine and arginine contacts to the triphosphate. Substrate binding promotes the association of trimers into hexamers and the transition of the hexamers from a loose to a tighter arrangement. Genetic experiments in mice show that loss of Cdadc1 is surprisingly well tolerated, even in the absence of the dCMP deaminase Dctd that is considered as the main source of dUMP, the precursor of dTTP.
History
DepositionNov 18, 2024-
Header (metadata) releaseApr 30, 2025-
Map releaseApr 30, 2025-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52125.png

Downloads & links

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Map

FileDownload / File: emd_52125.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.81 Å/pix.
x 256 pix.
= 207.36 Å		0.81 Å/pix.
x 256 pix.
= 207.36 Å		0.81 Å/pix.
x 256 pix.
= 207.36 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.81 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-1.9824264 - 2.5813208
Average (Standard dev.)-0.0011286265 (±0.071065806)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 207.36 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_52125_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_52125_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human CDADC1 trimer without a ligand (solution with 5mdCTP)

EntireName: Human CDADC1 trimer without a ligand (solution with 5mdCTP)
Components
  • Complex: Human CDADC1 trimer without a ligand (solution with 5mdCTP)
    • Protein or peptide: Human CDADC1

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Supramolecule #1: Human CDADC1 trimer without a ligand (solution with 5mdCTP)

SupramoleculeName: Human CDADC1 trimer without a ligand (solution with 5mdCTP)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 182 KDa

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Macromolecule #1: Human CDADC1

MacromoleculeName: Human CDADC1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MGSSHHHHHH SSGLVPRGSH MKEAGQMQNL ESARAGRSVS TQTGSMTGQI PRLSKVNLFT LLSLWMELFP AEAQRQKSQK NEEGKHGPLG DNEERTRVST DKRQVKRTGL VVVKNMKIVG LHCSSEDLHA GQIALIKHGS RLKNCDLYFS RKPCSACLKM IVNAGVNRIS ...String:
MGSSHHHHHH SSGLVPRGSH MKEAGQMQNL ESARAGRSVS TQTGSMTGQI PRLSKVNLFT LLSLWMELFP AEAQRQKSQK NEEGKHGPLG DNEERTRVST DKRQVKRTGL VVVKNMKIVG LHCSSEDLHA GQIALIKHGS RLKNCDLYFS RKPCSACLKM IVNAGVNRIS YWPADPEISL LTEASSSEDA KLDAKAVERL KSNSRAHVCV LLQPLVCYMV QFVEETSYKC DFIQKITKTL PDANTDFYYE CKQERIKEYE MLFLVSNEEM HKQILMTIGL ENLCENPYFS NLRQNMKDLI LLLATVASSV PNFKHFGFYR SNPEQINEIH NQSLPQEIAR HCMVQARLLA YRTEDHKTGV GAVIWAEGKS RSCDGTGAMY FVGCGYNAFP VGSEYADFPH MDDKQKDREI RKFRYIIHAA QNALTFRCQE IKPEERSMIF VTKCPCDECV PLIKGAGIKQ IYAGDVDVGK KKADISYMRF GELEGVSKFT WQLNPSGAYG LEQNEPERRE NGVLRPVPQK EEQHQDKKLR LGIH

UniProtKB: Cytidine and dCMP deaminase domain-containing protein 1

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.8 mg/mL
BufferpH: 7.4
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 42.9 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.81 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 2793395
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationSoftware - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: AB INITIO MODEL

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