› 1oy0

X-ray diffraction
2.8Å resolution

The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping

Released:
DOI: 10.2210/pdb1oy0/pdb
PDB entry 1oy0 coloured by chain, front view.
PDB entry 1oy0 coloured by chain, side view.
PDB entry 1oy0 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis.
Chaudhuri BN, Sawaya MR, Kim CY, Waldo GS, Park MS, Terwilliger TC, Yeates TO
Structure 11 753-64 (2003)
PMID: 12842039

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo decamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-methyl-2-oxobutanoate hydroxymethyltransferase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 281 amino acids
Theoretical weight: 29.37 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WIL7 (Residues: 1-281; Coverage: 100%)
Gene names: MTCY427.06, Rv2225, panB
Sequence domains: Ketopantoate hydroxymethyltransferase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

1 bound ligand:
Ligand MG 5 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 106.8Å b: 106.8Å c: 224.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.275
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

3 mentions without citation

Vitamin in the Crosshairs: Targeting Pantothenate and Coenzyme A Biosynthesis for New Antituberculosis Agents.
Butman et al. (2020)
2 more