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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-24566 | |||||||||
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Title | Substrate-bound Ura7 filament at low pH | |||||||||
![]() | Yeast CTP Synthase (Ura7) Filament bound to UTP/ATP at low pH | |||||||||
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![]() | glutaminase and amino-ligase / PROTEIN FIBRIL | |||||||||
Function / homology | ![]() CTP synthase (glutamine hydrolysing) / ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | 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 | ![]() | 8.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.4 KB 9.4 KB | Display Display | ![]() |
Images | ![]() | 80.1 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7rmfMC ![]() 7rkhC ![]() 7rl0C ![]() 7rl5C ![]() 7rmcC ![]() 7rmkC ![]() 7rmoC ![]() 7rmvC ![]() 7rnlC ![]() 7rnrC 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 (Ura7) Filament bound to UTP/ATP 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 Filament assembled with substrates
Entire | Name: CTP Synthase Filament assembled with substrates |
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Components |
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-Supramolecule #1: CTP Synthase Filament assembled with substrates
Supramolecule | Name: CTP Synthase Filament assembled with substrates / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() ![]() |
-Macromolecule #1: CTP synthase
Macromolecule | Name: CTP synthase / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO / EC number: CTP synthase (glutamine hydrolysing) |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 61.879922 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MKYVVVSGGV ISGIGKGVLA SSTGMLMKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV LDDGGETDLD LGNYERYLGV TLTKDHNIT TGKIYSHVIA KERKGDYLGK TVQIVPHLTN AIQDWIERVA KIPVDDTGME PDVCIIELGG TVGDIESAPF V EALRQFQF ...String: MKYVVVSGGV ISGIGKGVLA SSTGMLMKTL GLKVTSIKID PYMNIDAGTM SPLEHGECFV LDDGGETDLD LGNYERYLGV TLTKDHNIT TGKIYSHVIA KERKGDYLGK TVQIVPHLTN AIQDWIERVA KIPVDDTGME PDVCIIELGG TVGDIESAPF V EALRQFQF KVGKENFALI HVSLVPVIHG EQKTKPTQAA IKGLRSLGLV PDMIACRCSE TLDKPTIDKI AMFCHVGPEQ VV NVHDVNS TYHVPLLLLE QKMIDYLHAR LKLDEISLTE EEELLSKWKA TTGNFDETVK IALVGKYTNL KDSYLSVIKA LEH SSMKCR RKLDIKWVEA TDLEPEAQES NKTKFHEAWN MVSTADGILI PGGFGVRGTE GMVLAARWAR ENHIPFLGVC LGLQ IATIE FTRSVLGRKD SHSAEFYPDI DEKNHVVVFM MRLGLRPTFF QNETEWSQIK KLYGDVSEVH ERHRHRYEIN PKMVD ELEN NGLIFVGKDD TGKRCEILEL KNHPYYIATQ YHPEYTSKVL DPSKPFLGLV AASAGILQDV IEGKYDLEA UniProtKB: ![]() |
-Experimental details
-Structure determination
Method | ![]() |
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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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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 90.0 e/Å2 |
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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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 7.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 19706 |