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- EMDB-39759: The structure of type III CRISPR-associated deaminase apo form -

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Basic information

Entry
Database: EMDB / ID: EMD-39759
TitleThe structure of type III CRISPR-associated deaminase apo form
Map data
Sample
  • Complex: CRISPR-associated adenosine deaminase
    • Protein or peptide: Adenosine deaminase domain-containing protein
Keywordsdefense system / deaminase / IMMUNE SYSTEM
Function / homology
Function and homology information


inosine biosynthetic process / adenosine deaminase / hypoxanthine salvage / adenosine catabolic process / adenosine deaminase activity / nucleotide metabolic process / cytosol
Similarity search - Function
Adenosine deaminase domain / Adenosine deaminase / Adenosine/adenine deaminase / Metal-dependent hydrolase
Similarity search - Domain/homology
Biological speciesLimisphaera ngatamarikiensis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.26 Å
AuthorsChen MR / Li ZX / Xiao YB
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Science / Year: 2025
Title: Antiviral signaling of a type III CRISPR-associated deaminase.
Authors: Yutao Li / Zhaoxing Li / Purui Yan / Chenyang Hua / Jianping Kong / Wanqian Wu / Yurong Cui / Yan Duan / Shunxiang Li / Guanglei Li / Shunli Ji / Yijun Chen / Yucheng Zhao / Peng Yang / ...Authors: Yutao Li / Zhaoxing Li / Purui Yan / Chenyang Hua / Jianping Kong / Wanqian Wu / Yurong Cui / Yan Duan / Shunxiang Li / Guanglei Li / Shunli Ji / Yijun Chen / Yucheng Zhao / Peng Yang / Chunyi Hu / Meiling Lu / Meirong Chen / Yibei Xiao /
Abstract: Prokaryotes have evolved diverse defense strategies against viral infection, including foreign nucleic acid degradation by CRISPR-Cas systems and DNA and RNA synthesis inhibition through nucleotide ...Prokaryotes have evolved diverse defense strategies against viral infection, including foreign nucleic acid degradation by CRISPR-Cas systems and DNA and RNA synthesis inhibition through nucleotide pool depletion. Here, we report an antiviral mechanism of type III CRISPR-Cas-regulated adenosine triphosphate (ATP) depletion in which ATP is converted into inosine triphosphate (ITP) by CRISPR-Cas-associated adenosine deaminase (CAAD) upon activation by either cA or cA, followed by hydrolysis into inosine monophosphate (IMP) by Nudix hydrolase, ultimately resulting in cell growth arrest. The cryo-electron microscopy structures of CAAD in its apo and activated forms, together with biochemical evidence, revealed how cA or cA binds to the CRISPR-associated Rossmann fold (CARF) domain and abrogates CAAD autoinhibition, inducing substantial conformational changes that reshape the structure of CAAD and induce its deaminase activity. Our results reveal the mechanism of a CRISPR-Cas-regulated ATP depletion antiviral strategy.
History
DepositionApr 16, 2024-
Header (metadata) releaseDec 11, 2024-
Map releaseDec 11, 2024-
UpdateMar 5, 2025-
Current statusMar 5, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_39759.png

Downloads & links

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Map

FileDownload / File: emd_39759.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.92 Å/pix.
x 384 pix.
= 353.28 Å		0.92 Å/pix.
x 384 pix.
= 353.28 Å		0.92 Å/pix.
x 384 pix.
= 353.28 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.92 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.23314533 - 0.5815007
Average (Standard dev.)-0.0004938125 (±0.014870112)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 353.28 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_39759_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_39759_half_map_2.map
Projections & Slices
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Histogram

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Sample components

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Entire : CRISPR-associated adenosine deaminase

EntireName: CRISPR-associated adenosine deaminase
Components
  • Complex: CRISPR-associated adenosine deaminase
    • Protein or peptide: Adenosine deaminase domain-containing protein

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Supramolecule #1: CRISPR-associated adenosine deaminase

SupramoleculeName: CRISPR-associated adenosine deaminase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Limisphaera ngatamarikiensis (bacteria)

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Macromolecule #1: Adenosine deaminase domain-containing protein

MacromoleculeName: Adenosine deaminase domain-containing protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Limisphaera ngatamarikiensis (bacteria)
Molecular weightTheoretical: 70.859859 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MNVQAHLFVS LGTAPAIVPE AFLLPGARFV SVHVLTTERP DVTLIREFFR RHAPGVNLTI TRVAGFQDLK SEEDHFRFEE VMFRWFLAS RTGPEQRFVC LTGGFKTMSA AMQKAATVLG AAEVFHVLAD DCCVGPQGRL MPPSTLEEIL WARDQGHLHW I RLGPERGW ...String:
MNVQAHLFVS LGTAPAIVPE AFLLPGARFV SVHVLTTERP DVTLIREFFR RHAPGVNLTI TRVAGFQDLK SEEDHFRFEE VMFRWFLAS RTGPEQRFVC LTGGFKTMSA AMQKAATVLG AAEVFHVLAD DCCVGPQGRL MPPSTLEEIL WARDQGHLHW I RLGPERGW PQLRRIAPEQ FPLQVVEEKG DERRVQAEDR AFGTFLQDLL QRASRIAGAW EMLPELPFAD LATWSEGELA WL REPLDPR APADQRWVAG LPKIELHCHL GGFATHGELL RRVRNAAENP GKLPPLEEPR LPEGWPLPAQ PIPLAEYMKL GNA NGTALL RDPGCLREQC RLLYRHLVDQ GVCYAEVRCS PANYAEVRSP WDVLADIRAA FQECMEGART APGGLPACHV NLIL IATRR ASGDYRAAIA RHLALAVTAA EHWRDENACR VVGVDLAGYE DEKTRAHYFR EEFTAVHRCG LAVTVHAGEN DDAEG IWRA VFDLNARRLG HALSLGQSRE LLRSVADRGI GVELCPYANL QIKGFRLDGS DRAGPADPRH EAHAPGPYPL LDYLRE GVR VTVNTDNIGI SAASLTDNLL LAARLCPGLT RLDLLHLQRH ALETAFCTAT QRLTLLRRIS SGIPRPHHHH HH

UniProtKB: adenosine deaminase

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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

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.26 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 247410
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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