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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-24581 | |||||||||
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Title | Yeast CTP Synthase (Ura8) Bundle Bound to Substrates at Low pH | |||||||||
![]() | Yeast CTP Synthase (Ura8) Bundle bound to substrates at low pH | |||||||||
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![]() | glutaminase and amido-ligase / PROTEIN FIBRIL | |||||||||
Function / homology | ![]() CTP synthase (glutamine hydrolysing) / CTP synthase activity / cytoophidium / 'de novo' CTP biosynthetic process / pyrimidine nucleobase biosynthetic process / glutamine metabolic process / ATP binding / identical protein binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Hansen JM / Lynch EM | |||||||||
Funding support | 2 items
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![]() | ![]() Title: Cryo-EM structures of CTP synthase filaments reveal mechanism of pH-sensitive assembly during budding yeast starvation. Authors: Jesse M Hansen / Avital Horowitz / Eric M Lynch / Daniel P Farrell / Joel Quispe / Frank DiMaio / Justin M Kollman / ![]() Abstract: Many metabolic enzymes self-assemble into micron-scale filaments to organize and regulate metabolism. The appearance of these assemblies often coincides with large metabolic changes as in ...Many metabolic enzymes self-assemble into micron-scale filaments to organize and regulate metabolism. The appearance of these assemblies often coincides with large metabolic changes as in development, cancer, and stress. Yeast undergo cytoplasmic acidification upon starvation, triggering the assembly of many metabolic enzymes into filaments. However, it is unclear how these filaments assemble at the molecular level and what their role is in the yeast starvation response. CTP Synthase (CTPS) assembles into metabolic filaments across many species. Here, we characterize in vitro polymerization and investigate in vivo consequences of CTPS assembly in yeast. Cryo-EM structures reveal a pH-sensitive assembly mechanism and highly ordered filament bundles that stabilize an inactive state of the enzyme, features unique to yeast CTPS. Disruption of filaments in cells with non-assembly or pH-insensitive mutations decreases growth rate, reflecting the importance of regulated CTPS filament assembly in homeotstasis. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 10.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 10.7 KB 10.7 KB | Display Display | ![]() |
Images | ![]() | 90.7 KB | ||
Filedesc metadata | ![]() | 5.5 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 351.4 KB | Display | ![]() |
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Full document | ![]() | 351 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 9.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7rnrMC ![]() 7rkhC ![]() 7rl0C ![]() 7rl5C ![]() 7rmcC ![]() 7rmfC ![]() 7rmkC ![]() 7rmoC ![]() 7rmvC ![]() 7rnlC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Yeast CTP Synthase (Ura8) Bundle bound to substrates at low pH | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : CTP Synthase Bundle assembled with Substrates
Entire | Name: CTP Synthase Bundle assembled with Substrates |
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Components |
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-Supramolecule #1: CTP Synthase Bundle assembled with Substrates
Supramolecule | Name: CTP Synthase Bundle assembled with Substrates / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: CTP synthase
Macromolecule | Name: CTP synthase / type: protein_or_peptide / ID: 1 / Number of copies: 20 / Enantiomer: LEVO / EC number: CTP synthase (glutamine hydrolysing) |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 62.439168 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKYVVVSGGV ISGIGKGVLA SSTGMLLKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV LDDGGETDLD LGNYERYLGI TLSRDHNIT TGKIYSHVIS RERRGDYLGK TVQIVPHLTN AIQDWIQRVS KIPVDDTGLE PDVCIIELGG TVGDIESAPF V EALRQFQF ...String: MKYVVVSGGV ISGIGKGVLA SSTGMLLKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV LDDGGETDLD LGNYERYLGI TLSRDHNIT TGKIYSHVIS RERRGDYLGK TVQIVPHLTN AIQDWIQRVS KIPVDDTGLE PDVCIIELGG TVGDIESAPF V EALRQFQF EVGRENFALI HVSLVPVIHG EQKTKPTQAA IKDLRSLGLI PDMIACRCSE ELNRSTIDKI AMFCHVGPEQ VV NVHDVNS TYHVPLLLLK QHMIDYLHSR LKLGEVPLTL EDKERGSQLL TNWENMTKNL DDSDDVVKIA LVGKYTNLKD SYL SVTKSL EHASMKCRRQ LEILWVEASN LEPETQEVDK NKFHDSWNKL SSADGILVPG GFGTRGIEGM ILAAKWARES GVPF LGVCL GLQVAAIEFA RNVIGRPNSS STEFLDETLL APEDQVVITM RLGLRPTIFQ PNSEWSNIRK LYGEVNEVHE RHRHR YEIN PKIVNDMESR GFIFVGKDET GQRCEIFELK GHPYYVGTQY HPEYTSKVLE PSRPFWGLVA AASGTLGEVI KDINL UniProtKB: CTP synthase |
-Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 20 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Macromolecule #3: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 40 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #4: URIDINE 5'-TRIPHOSPHATE
Macromolecule | Name: URIDINE 5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 20 / Formula: UTP |
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Molecular weight | Theoretical: 484.141 Da |
Chemical component information | ![]() ChemComp-UTP: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 6 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 90.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY |
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Final reconstruction | Applied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: OTHER / Details: FSCref0.5 (Phenix Density Modification) / Number images used: 21220 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |