› 2gci

X-ray diffraction
1.6Å resolution

The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety

Released:
DOI: 10.2210/pdb2gci/pdb
PDB entry 2gci coloured by chain, front view.
PDB entry 2gci coloured by chain, side view.
PDB entry 2gci coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The catalysis of the 1,1-proton transfer by alpha-methyl-acyl-CoA racemase is coupled to a movement of the fatty acyl moiety over a hydrophobic, methionine-rich surface.
Bhaumik P, Schmitz W, Hassinen A, Hiltunen JK, Conzelmann E, Wierenga RK
J Mol Biol 367 1145-61 (2007)
PMID: 17320106

Function and Biology Details

Reaction catalysed: 
(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-methylacyl-CoA racemase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 360 amino acids
Theoretical weight: 38.72 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O06543 (Residues: 1-360; Coverage: 100%)
Gene names: Rv1143, mcr
Sequence domains: CoA-transferase family III
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MRR 4 x MRR
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: C2
Unit cell:
a: 180.7Å b: 79.81Å c: 118.06Å
α: 90° β: 89.93° γ: 90°
R-values:
R R work R free
0.212 0.21 0.244
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism.
Van Veldhoven PP. (2010)
2 more

1 mention without citation

Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.
Lloyd et al. (2021)