› 1hzp

X-ray diffraction
2.1Å resolution

Crystal Structure of the Myobacterium Tuberculosis Beta-Ketoacyl-Acyl Carrier Protein Synthase III

Released:
DOI: 10.2210/pdb1hzp/pdb
PDB entry 1hzp coloured by chain, front view.
PDB entry 1hzp coloured by chain, side view.
PDB entry 1hzp coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III.
Scarsdale JN, Kazanina G, He X, Reynolds KA, Wright HT
J Biol Chem 276 20516-22 (2001)
PMID: 11278743

Function and Biology Details

Reaction catalysed: 
Dodecanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO(2)
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-161855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mycobacterial beta-ketoacyl-[acyl-carrier-protein] synthase III Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 34.9 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNG3 (Residues: 1-335; Coverage: 100%)
Gene names: MTCY25D10.12c, Rv0533c, fabH
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand DAO 1 x DAO
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 64.082Å b: 54.779Å c: 89.152Å
α: 90° β: 90.3° γ: 90°
R-values:
R R work R free
0.222 0.222 0.262
Expression system: Escherichia coli

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Citations

18 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
17 more

6 mentions without citation

The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue.
Veyron-Churlet et al. (2009)
5 more