› 7xmu

Electron Microscopy
2.3Å resolution

E.coli phosphoribosylpyrophosphate (PRPP) synthetase type A filament bound with ADP, Pi and R5P

Released:
DOI: 10.2210/pdb7xmu/pdb
PDB entry 7xmu coloured by chain, front view.
PDB entry 7xmu coloured by chain, side view.
PDB entry 7xmu coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. MG1655
Primary publication:
Filamentation modulates allosteric regulation of PRPS.
Hu HH, Lu GM, Chang CC, Li Y, Zhong J, Guo CJ, Zhou X, Yin B, Zhang T, Liu JL
OpenAccess logo Elife 11 (2022)
PMID: 35736577
Related structures: EMD-33305

Function and Biology Details

Reaction catalysed: 
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-532005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-phosphate pyrophosphokinase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 321 amino acids
Theoretical weight: 35.08 KDa
Source organism: Escherichia coli str. K-12 substr. MG1655
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P0A717 (Residues: 1-315; Coverage: 100%)
Gene names: JW1198, b1207, prs, prsA
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand HSX 6 x HSX
Ligand MG 12 x MG
Ligand PO4 6 x PO4
Ligand ADP 12 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.3Å
Relevant EMDB volumes: EMD-33305
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

1 review citation

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

3 mentions without citation

Human PRPS1 filaments stabilize allosteric sites to regulate activity.
Hvorecny et al. (2023)
2 more