› 5z9o

X-ray diffraction
2.7Å resolution

The crystal structure of Cyclopropane-fatty-acyl-phospholipid synthase from Lactobacillus acidophilus

Released:
DOI: 10.2210/pdb5z9o/pdb
PDB entry 5z9o coloured by chain, front view.
PDB entry 5z9o coloured by chain, side view.
PDB entry 5z9o coloured by chain, top view.
Source organism: Lactobacillus acidophilus NCFM
Primary publication:
Crystal structure of bacterial cyclopropane-fatty-acyl-phospholipid synthase with phospholipid.
Ma Y, Pan C, Wang Q
J Biochem 166 139-147 (2019)
PMID: 30828715

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclopropane-fatty-acyl-phospholipid synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 399 amino acids
Theoretical weight: 46.03 KDa
Source organism: Lactobacillus acidophilus NCFM
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5FJM0 (Residues: 1-393; Coverage: 100%)
Gene name: LBA1274
Sequence domains: Mycolic acid cyclopropane synthetase

Ligands and Environments

2 bound ligands:
Ligand CO3 2 x CO3
Ligand EPH 2 x EPH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P61
Unit cell:
a: 120.982Å b: 120.982Å c: 163.487Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.213
Expression system: Escherichia coli

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Citations

1 review citation

Methyltransferases: Functions and Applications.
Abdelraheem et al. (2022)
4 other articles

3 mentions without citation

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