› 3b6z

X-ray diffraction
1.88Å resolution

Lovastatin polyketide enoyl reductase (LovC) complexed with 2'-phosphoadenosyl isomer of crotonoyl-CoA

Released:
DOI: 10.2210/pdb3b6z/pdb
PDB entry 3b6z coloured by chain, front view.
PDB entry 3b6z coloured by chain, side view.
PDB entry 3b6z coloured by chain, top view.
Source organism: Aspergillus terreus
Primary publication:
Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis.
Ames BD, Nguyen C, Bruegger J, Smith P, Xu W, Ma S, Wong E, Wong S, Xie X, Li JW, Vederas JC, Tang Y, Tsai SC
Proc Natl Acad Sci U S A 109 11144-9 (2012)
PMID: 22733743

Function and Biology Details

Reaction catalysed: 
9 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO(2) + 11 NADP(+) + S-adenosyl-L-homocysteine + 6 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195404 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lovastatin nonaketide synthase, enoyl reductase component lovC Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 40.62 KDa
Source organism: Aspergillus terreus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y7D0 (Residues: 1-363; Coverage: 100%)
Gene name: lovC
Sequence domains: Alcohol dehydrogenase GroES-like domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CO7 1 x CO7
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 44.334Å b: 54.867Å c: 171.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.171 0.221
Expression system: Escherichia coli

Quick links

Citations

14 review citations

The structures of type I polyketide synthases.
Keatinge-Clay AT. (2012)
13 more

1 mention without citation

Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis.
Ames et al. (2012)