› 3sez

X-ray diffraction
2.65Å resolution

Crystal structure of C176A mutant of glutamine-dependent NAD+ synthetase from M. tuberculosis in complex with ATP and NaAD+

Released:
DOI: 10.2210/pdb3sez/pdb
PDB entry 3sez coloured by chain, front view.
PDB entry 3sez coloured by chain, side view.
PDB entry 3sez coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase.
Chuenchor W, Doukov TI, Resto M, Chang A, Gerratana B
Biochem J 443 417-26 (2012)
PMID: 22280445

Function and Biology Details

Reaction catalysed: 
ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine-dependent NAD(+) synthetase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 680 amino acids
Theoretical weight: 74.82 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WJJ3 (Residues: 1-679; Coverage: 100%)
Gene names: MTCY428.08, Rv2438c, nadE
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 4 x ATP
Ligand DND 4 x DND
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P41212
Unit cell:
a: 178.407Å b: 178.407Å c: 216.303Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.214
Expression system: Escherichia coli

Quick links

Citations

1 review citation

A structural perspective on the PP-loop ATP pyrophosphatase family.
Fellner et al. (2018)
8 other articles