› 1kpi

X-ray diffraction
2.65Å resolution

Crystal Structure of mycolic acid cyclopropane synthase CmaA2 complexed with SAH and DDDMAB

Released:
DOI: 10.2210/pdb1kpi/pdb
PDB entry 1kpi coloured by chain, front view.
PDB entry 1kpi coloured by chain, side view.
PDB entry 1kpi coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis.
Huang CC, Smith CV, Glickman MS, Jacobs WR, Sacchettini JC
J Biol Chem 277 11559-69 (2002)
PMID: 11756461

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-161938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclopropane mycolic acid synthase 2 Chain: A
Molecule details ›
Chain: A
Length: 302 amino acids
Theoretical weight: 34.64 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WPB5 (Residues: 1-302; Coverage: 100%)
Gene names: CMAS-2, MTCY20G9.30c, Rv0503c, cma2, cmaA2
Sequence domains: Mycolic acid cyclopropane synthetase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
3 bound ligands:
Ligand CO3 1 x CO3
Ligand SO4 4 x SO4
Ligand 10A 1 x 10A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: I4122
Unit cell:
a: 106.71Å b: 106.71Å c: 227.498Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

Antituberculosis drugs: ten years of research.
Janin YL. (2007)
21 more

11 mentions without citation

Diversity of the reaction mechanisms of SAM-dependent enzymes.
Sun et al. (2021)
10 more