› 2a81

X-ray diffraction
3.15Å resolution

carboxymethylproline synthase (CarB) from pectobacterium carotovora, complexed with acetyl CoA and bicine

Released:
DOI: 10.2210/pdb2a81/pdb
PDB entry 2a81 coloured by chain, front view.
PDB entry 2a81 coloured by chain, side view.
PDB entry 2a81 coloured by chain, top view.
Source organism: Pectobacterium carotovorum
Primary publication:
Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis.
Sleeman MC, Sorensen JL, Batchelar ET, McDonough MA, Schofield CJ
J Biol Chem 280 34956-65 (2005)
PMID: 16096274

Function and Biology Details

Reaction catalysed: 
Malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H(2)O = CoA + (2S,5S)-5-carboxymethylproline + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxymethylproline synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 250 amino acids
Theoretical weight: 27.61 KDa
Source organism: Pectobacterium carotovorum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9XB60 (Residues: 1-250; Coverage: 100%)
Gene name: carB
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACO 1 x ACO
Ligand BCN 1 x BCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P63
Unit cell:
a: 139.605Å b: 139.605Å c: 78.546Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The enzymes of β-lactam biosynthesis.
Hamed et al. (2013)
1 more

1 mention without citation

Structural and biophysical characterization of BoxC from Burkholderia xenovorans LB400: a novel ring-cleaving enzyme in the crotonase superfamily.
Bains et al. (2009)