› 3dla

X-ray diffraction
2.35Å resolution

X-ray crystal structure of glutamine-dependent NAD+ synthetase from Mycobacterium tuberculosis bound to NaAD+ and DON

Released:
DOI: 10.2210/pdb3dla/pdb
PDB entry 3dla coloured by chain, front view.
PDB entry 3dla coloured by chain, side view.
PDB entry 3dla coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Regulation of active site coupling in glutamine-dependent NAD(+) synthetase.
LaRonde-LeBlanc N, Resto M, Gerratana B
Nat Struct Mol Biol 16 421-9 (2009)
PMID: 19270703

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: 74.86 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

3 bound ligands:
Ligand DND 4 x DND
Ligand ONL 4 x ONL
Ligand GOL 15 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P41212
Unit cell:
a: 178.13Å b: 178.13Å c: 215.177Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.246
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets.
Bi et al. (2011)
3 more

10 mentions without citation

Adenylating enzymes in Mycobacterium tuberculosis as drug targets.
Duckworth et al. (2012)
9 more