› 5iiq

X-ray diffraction
3.03Å resolution

Structure of the SPX-TTM domain fragment of the yeast inorganic polyphophate polymerase Vtc4 (form B).

Released:
DOI: 10.2210/pdb5iiq/pdb
PDB entry 5iiq coloured by chain, front view.
PDB entry 5iiq coloured by chain, side view.
PDB entry 5iiq coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains.
Wild R, Gerasimaite R, Jung JY, Truffault V, Pavlovic I, Schmidt A, Saiardi A, Jessen HJ, Poirier Y, Hothorn M, Mayer A
Science 352 986-90 (2016)
PMID: 27080106

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: 485 amino acids
Theoretical weight: 56.95 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P47075 (Residues: 2-480; Coverage: 66%)
Gene names: J1345, PHM3, VTC4, YJL012C
Sequence domains: VTC domain
Structure domains: VTC, catalytic tunnel domain

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand POP 1 x POP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P6422
Unit cell:
a: 92.041Å b: 92.041Å c: 301.732Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.225 0.262
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

65 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
64 more

2 mentions without citation

The macro domain as fusion tag for carrier-driven crystallization.
Wild et al. (2017)
1 more