› 5lot

X-ray diffraction
2.25Å resolution

Crystal structure of SCP2 thiolase from Leishmania mexicana. Complex of the C123A mutant with acetyl-CoA.

Released:
DOI: 10.2210/pdb5lot/pdb
PDB entry 5lot coloured by chain, front view.
PDB entry 5lot coloured by chain, side view.
PDB entry 5lot coloured by chain, top view.
Source organism: Leishmania mexicana MHOM/GT/2001/U1103
Primary publication:
Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.
Harijan RK, Kiema TR, Syed SM, Qadir I, Mazet M, Bringaud F, Michels PAM, Wierenga RK
Protein Eng Des Sel 30 225-233 (2017)
PMID: 28062645

Function and Biology Details

Reaction catalysed: 
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123156 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
propanoyl-CoA C-acyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 457 amino acids
Theoretical weight: 49.23 KDa
Source organism: Leishmania mexicana MHOM/GT/2001/U1103
Expression system: Escherichia coli
UniProt:
  • Canonical: E9AW84 (Residues: 1-441; Coverage: 100%)
Gene name: LMXM_23_0690
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand ACO 3 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 79.701Å b: 89.889Å c: 126.332Å
α: 90° β: 105.78° γ: 90°
R-values:
R R work R free
0.216 0.214 0.255
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The 3-ketoacyl-CoA thiolase: an engineered enzyme for carbon chain elongation of chemical compounds.
Liu et al. (2020)