› 1qap

X-ray diffraction
2.8Å resolution

QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE WITH BOUND QUINOLINIC ACID

Released:
DOI: 10.2210/pdb1qap/pdb
PDB entry 1qap coloured by chain, front view.
PDB entry 1qap coloured by chain, side view.
PDB entry 1qap coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase.
Eads JC, Ozturk D, Wexler TB, Grubmeyer C, Sacchettini JC
Structure 5 47-58 (1997)
PMID: 9016724

Function and Biology Details

Reaction catalysed: 
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151604 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinate-nucleotide pyrophosphorylase [carboxylating] Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 32.48 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30012 (Residues: 2-297; Coverage: 100%)
Gene names: STM0145, nadC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NTM 2 x NTM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 81.4Å b: 81.4Å c: 217.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.274
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Fold change in evolution of protein structures.
Grishin NV. (2001)
5 more

2 mentions without citation

Biogenesis and Homeostasis of Nicotinamide Adenine Dinucleotide Cofactor.
Osterman A. (2009)
1 more