› 3g3t

X-ray diffraction
1.85Å resolution

Crystal structure of a eukaryotic polyphosphate polymerase in complex with orthophosphate

Released:
DOI: 10.2210/pdb3g3t/pdb
PDB entry 3g3t coloured by chain, front view.
PDB entry 3g3t coloured by chain, side view.
PDB entry 3g3t coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase.
Hothorn M, Neumann H, Lenherr ED, Wehner M, Rybin V, Hassa PO, Uttenweiler A, Reinhardt M, Schmidt A, Seiler J, Ladurner AG, Herrmann C, Scheffzek K, Mayer A
Science 324 513-6 (2009)
PMID: 19390046

Function and Biology Details

Reaction catalysed: 
ATP + (phosphate)(n) = ADP + (phosphate)(n+1)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar transporter chaperone complex subunit 4 Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.77 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P47075 (Residues: 189-480; Coverage: 41%)
Gene names: J1345, PHM3, VTC4, YJL012C
Sequence domains: VTC domain
Structure domains: VTC, catalytic tunnel domain

Ligands and Environments

2 bound ligands:
Ligand PO4 4 x PO4
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6322
Unit cell:
a: 136.11Å b: 136.11Å c: 84.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.235
Expression system: Escherichia coli

Quick links

Citations

49 review citations

Polyphosphate: an ancient molecule that links platelets, coagulation, and inflammation.
Morrissey et al. (2012)
48 more

4 mentions without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)
3 more