› 1ytd

X-ray diffraction
2.8Å resolution

Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum, Native Structure

Released:
DOI: 10.2210/pdb1ytd/pdb
PDB entry 1ytd coloured by chain, front view.
PDB entry 1ytd coloured by chain, side view.
PDB entry 1ytd coloured by chain, top view.
Source organism: Thermoplasma acidophilum DSM 1728
Primary publication:
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.
Shin DH, Oganesyan N, Jancarik J, Yokota H, Kim R, Kim SH
J Biol Chem 280 18326-35 (2005)
PMID: 15753098

Function and Biology Details

Reaction catalysed: 
Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H(2)O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190847 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative nicotinate phosphoribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 398 amino acids
Theoretical weight: 43.7 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HJ28 (Residues: 1-392; Coverage: 100%)
Gene name: Ta1145
Sequence domains: Quinolinate phosphoribosyl transferase, C-terminal domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P6322
Unit cell:
a: 136.024Å b: 136.024Å c: 119.733Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.198 0.246
Expression system: Escherichia coli

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Citations

6 review citations

Disulfides as redox switches: from molecular mechanisms to functional significance.
Wouters et al. (2010)
5 more

2 mentions without citation

Streptococcus pyogenes quinolinate-salvage pathway-structural and functional studies of quinolinate phosphoribosyl transferase and NH3 -dependent NAD+ synthetase.
Booth et al. (2017)
1 more