› 7rkh

Electron Microscopy
2.8Å resolution

Yeast CTP Synthase (URA8) tetramer bound to ATP/UTP at neutral pH

Released:
DOI: 10.2210/pdb7rkh/pdb
PDB entry 7rkh coloured by chain, front view.
PDB entry 7rkh coloured by chain, side view.
PDB entry 7rkh coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Cryo-EM structures of CTP synthase filaments reveal mechanism of pH-sensitive assembly during budding yeast starvation.
Hansen JM, Horowitz A, Lynch EM, Farrell DP, Quispe J, DiMaio F, Kollman JM
OpenAccess logo Elife 10 (2021)
PMID: 34734801
Related structures: EMD-24497

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105569 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 559 amino acids
Theoretical weight: 62.44 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:
Ligand UTP 4 x UTP
Ligand ATP 4 x ATP
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.8Å
Relevant EMDB volumes: EMD-24497
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Greater than the sum of parts: Mechanisms of metabolic regulation by enzyme filaments.
Hvorecny et al. (2023)
2 more

1 mention without citation

Cryo-EM structures of CTP synthase filaments reveal mechanism of pH-sensitive assembly during budding yeast starvation.
Hansen et al. (2021)