› 6pk4

Electron Microscopy
3.5Å resolution

cryoEM structure of the substrate-bound human CTP synthase 2 filament

Released:
DOI: 10.2210/pdb6pk4/pdb
PDB entry 6pk4 coloured by chain, front view.
PDB entry 6pk4 coloured by chain, side view.
PDB entry 6pk4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Coupled structural transitions enable highly cooperative regulation of human CTPS2 filaments.
Lynch EM, Kollman JM
Nat Struct Mol Biol 27 42-48 (2020)
PMID: 31873303
Related structures: EMD-20354

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192557 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 586 amino acids
Theoretical weight: 65.76 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q9NRF8 (Residues: 1-586; Coverage: 100%)
Gene name: CTPS2
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand UTP 4 x UTP
Ligand ATP 4 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.5Å
Relevant EMDB volumes: EMD-20354
Expression system: Saccharomyces cerevisiae

Quick links

Citations

4 review citations

Filament formation by metabolic enzymes-A new twist on regulation.
Lynch et al. (2020)
3 more

3 mentions without citation

Coupled structural transitions enable highly cooperative regulation of human CTPS2 filaments.
Lynch et al. (2020)
2 more