› 1n2o

X-ray diffraction
2.1Å resolution

Crystal Structure of Pantothenate Synthetase from M. tuberculosis, low occupancy of beta-alanine at the pantoate binding sites

Released:
DOI: 10.2210/pdb1n2o/pdb
PDB entry 1n2o coloured by chain, front view.
PDB entry 1n2o coloured by chain, side view.
PDB entry 1n2o coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate.
Wang S, Eisenberg D
Protein Sci 12 1097-108 (2003)
PMID: 12717031

Function and Biology Details

Reaction catalysed: 
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161641 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pantothenate synthetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 300 amino acids
Theoretical weight: 31.5 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WIL5 (Residues: 1-300; Coverage: 97%)
Gene names: MTCY07H7B.20, Rv3602c, panC
Sequence domains: Pantoate-beta-alanine ligase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand BAL 2 x BAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P212121
Unit cell:
a: 69.747Å b: 98.648Å c: 82.102Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

Coenzyme A biosynthesis: an antimicrobial drug target.
Spry et al. (2008)
13 more

2 mentions without citation

Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate.
Wang et al. (2003)
1 more