› 1tfu

X-ray diffraction
1.99Å resolution

phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb1tfu/pdb
PDB entry 1tfu coloured by chain, front view.
PDB entry 1tfu coloured by chain, side view.
PDB entry 1tfu coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Morris VK, Izard T
Protein Sci 13 2547-52 (2004)
PMID: 15322293

Function and Biology Details

Reaction catalysed: 
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphopantetheine adenylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.16 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPA5 (Residues: 1-157; Coverage: 98%)
Gene names: MTCY349.22, Rv2965c, coaD, kdtB, u0002e
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 98.623Å b: 98.623Å c: 114.811Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.258
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

5 mentions without citation

Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Morris et al. (2004)
4 more