› 3vvm

X-ray diffraction
1.7Å resolution

Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway

Released:
DOI: 10.2210/pdb3vvm/pdb
PDB entry 3vvm coloured by chain, front view.
PDB entry 3vvm coloured by chain, side view.
PDB entry 3vvm coloured by chain, top view.
Source organism: Streptomyces lavendulae subsp. lavendulae
Primary publication:
Crystallographic study to determine the substrate specificity of an L-serine-acetylating enzyme found in the D-cycloserine biosynthetic pathway.
Oda K, Matoba Y, Kumagai T, Noda M, Sugiyama M
J Bacteriol 195 1741-9 (2013)
PMID: 23396912

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112459 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-serine/homoserine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 42.46 KDa
Source organism: Streptomyces lavendulae subsp. lavendulae
Expression system: Escherichia coli
UniProt:
  • Canonical: D2Z028 (Residues: 1-374; Coverage: 100%)
Gene names: dcsE, metX
Sequence domains: alpha/beta hydrolase fold
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 46.56Å b: 102.33Å c: 147.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.214
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis.
Bastard et al. (2017)
9 more

1 mention without citation

Crystallographic study to determine the substrate specificity of an L-serine-acetylating enzyme found in the D-cycloserine biosynthetic pathway.
Oda et al. (2013)