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- EMDB-65191: human CTPS1 with 2CTP and DON -

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Basic information

Entry
Database: EMDB / ID: EMD-65191
Titlehuman CTPS1 with 2CTP and DON
Map data
Sample
  • Complex: hCTPS1 with 2CTP and DON
    • Protein or peptide: CTP synthase 1
  • Ligand: CYTIDINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
KeywordsCTP synthase / CTP / DON / cytosolic protein / STRUCTURAL PROTEIN
Function / homology
Function and homology information


cytoophidium / CTP synthase (glutamine hydrolysing) / CTP synthase activity / 'de novo' CTP biosynthetic process / pyrimidine nucleobase biosynthetic process / Interconversion of nucleotide di- and triphosphates / CTP biosynthetic process / nucleobase-containing compound metabolic process / B cell proliferation / T cell proliferation ...cytoophidium / CTP synthase (glutamine hydrolysing) / CTP synthase activity / 'de novo' CTP biosynthetic process / pyrimidine nucleobase biosynthetic process / Interconversion of nucleotide di- and triphosphates / CTP biosynthetic process / nucleobase-containing compound metabolic process / B cell proliferation / T cell proliferation / response to xenobiotic stimulus / ATP binding / identical protein binding / membrane / cytosol / cytoplasm
Similarity search - Function
CTP synthase / CTP synthase, N-terminal / CTP synthase GATase domain / CTP synthase N-terminus / Glutamine amidotransferase / Glutamine amidotransferase class-I / Glutamine amidotransferase type 1 domain profile. / Class I glutamine amidotransferase-like / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsGuo CJ / Bao XJ / Liu JL
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Cell Biosci / Year: 2025
Title: Filamentation of hCTPS1 with CTP.
Authors: Chen-Jun Guo / Xiaojie Bao / Ji-Long Liu /
Abstract: CTP synthase (CTPS) is a key enzyme in de novo CTP synthesis, playing a critical role in nucleotide metabolism and cellular proliferation. Human CTPS1 (hCTPS1), one of the two CTPS isoforms, is ...CTP synthase (CTPS) is a key enzyme in de novo CTP synthesis, playing a critical role in nucleotide metabolism and cellular proliferation. Human CTPS1 (hCTPS1), one of the two CTPS isoforms, is essential for immune responses and is highly expressed in proliferating cells, making it a promising therapeutic target for immune-related diseases and cancer. Despite its importance, the regulatory mechanisms governing hCTPS1 activity remain poorly understood. Here, we reveal that CTP, the product of CTPS, acts as a key regulator for hCTPS1 filamentation. Using cryo-electron microscopy (cryo-EM), we resolve the high-resolution structure of CTP-bound hCTPS1 filaments, uncovering the molecular details of CTP binding and its role in filament assembly. Importantly, we demonstrate that CTP generated from the enzymatic reaction does not trigger filament disassembly, suggesting a conserved regulatory pattern. Furthermore, by analyzing the binding modes of two distinct CTP-binding pockets, we provide evidence that this filamentation mechanism is evolutionarily conserved across species, particularly in eukaryotic CTPS. Our findings not only elucidate a novel regulatory mechanism of hCTPS1 activity but also deepen the understanding of how metabolic enzymes utilize filamentation as a conserved strategy for functional regulation. This study opens new avenues for targeting hCTPS1 in therapeutic interventions.
History
DepositionJun 28, 2025-
Header (metadata) releaseDec 24, 2025-
Map releaseDec 24, 2025-
UpdateDec 24, 2025-
Current statusDec 24, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_65191.png

Downloads & links

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Map

FileDownload / File: emd_65191.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 250 pix.
= 205. Å		0.82 Å/pix.
x 250 pix.
= 205. Å		0.82 Å/pix.
x 250 pix.
= 205. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.014
Minimum - Maximum-0.075705506 - 0.10742802
Average (Standard dev.)0.00012321705 (±0.00501456)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions250250250
Spacing250250250
CellA=B=C: 205.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_65191_msk_1.map
Projections & Slices
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Histogram

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Half map: #2

Fileemd_65191_half_map_1.map
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Half map: #1

Fileemd_65191_half_map_2.map
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Sample components

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Entire : hCTPS1 with 2CTP and DON

EntireName: hCTPS1 with 2CTP and DON
Components
  • Complex: hCTPS1 with 2CTP and DON
    • Protein or peptide: CTP synthase 1
  • Ligand: CYTIDINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: hCTPS1 with 2CTP and DON

SupramoleculeName: hCTPS1 with 2CTP and DON / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: CTP synthase 1

MacromoleculeName: CTP synthase 1 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: CTP synthase (glutamine hydrolysing)
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 66.777297 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV LDDGGEVDLD LGNYERFLDI RLTKDNNLT TGKIYQYVIN KERKGDYLGK TVQVVPHITD AIQEWVMRQA LIPVDEDGLE PQVCVIELGG TVGDIESMPF I EAFRQFQF ...String:
MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV LDDGGEVDLD LGNYERFLDI RLTKDNNLT TGKIYQYVIN KERKGDYLGK TVQVVPHITD AIQEWVMRQA LIPVDEDGLE PQVCVIELGG TVGDIESMPF I EAFRQFQF KVKRENFCNI HVSLVPQPSS TGEQKTKPTQ NSVRELRGLG LSPDLVVCRC SNPLDTSVKE KISMFCHVEP EQ VICVHDV SSIYRVPLLL EEQGVVDYFL RRLDLPIERQ PRKMLMKWKE MADRYDRLLE TCSIALVGKY TKFSDSYASV IKA LEHSAL AINHKLEIKY IDSADLEPIT SQEEPVRYHE AWQKLCSAHG VLVPGGFGVR GTEGKIQAIA WARNQKKPFL GVCL GMQLA VVEFSRNVLG WQDANSTEFD PTTSHPVVVD MPEHNPGQMG GTMRLGKRRT LFQTKNSVMR KLYGDADYLE ERHRH RFEV NPVWKKCLEE QGLKFVGQDV EGERMEIVEL EDHPFFVGVQ YHPEFLSRPI KPSPPYFGLL LASVGRLSHY LQKGCR LSP RDTYSDRSGS SSPDSEITEL KFPSINHD

UniProtKB: CTP synthase 1

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Macromolecule #2: CYTIDINE-5'-TRIPHOSPHATE

MacromoleculeName: CYTIDINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 8 / Formula: CTP
Molecular weightTheoretical: 483.156 Da
Chemical component information

ChemComp-CTP:
CYTIDINE-5'-TRIPHOSPHATE

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 8 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE / Details: AlphaFold
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: UCSF Chimera / Number images used: 989280
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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