› 1ysl

X-ray diffraction
1.9Å resolution

Crystal structure of HMG-CoA synthase from Enterococcus faecalis with AcetoAcetyl-CoA ligand.

Released:
DOI: 10.2210/pdb1ysl/pdb
PDB entry 1ysl coloured by chain, front view.
PDB entry 1ysl coloured by chain, side view.
PDB entry 1ysl coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA.
Steussy CN, Vartia AA, Burgner JW, Sutherlin A, Rodwell VW, Stauffacher CV
Biochemistry 44 14256-67 (2005)
PMID: 16245942

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190290 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hydroxymethylglutaryl-CoA synthase Chain: A
Molecule details ›
Chain: A
Length: 402 amino acids
Theoretical weight: 44.31 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FD71 (Residues: 1-383; Coverage: 100%)
Gene name: mvaS
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1
Hydroxymethylglutaryl-CoA synthase Chain: B
Molecule details ›
Chain: B
Length: 402 amino acids
Theoretical weight: 44.28 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FD71 (Residues: 1-383; Coverage: 100%)
Gene name: mvaS
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 1 x COA
3 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 2 x GOL
Ligand AAE 1 x AAE
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: I222
Unit cell:
a: 105.3Å b: 109.013Å c: 140.799Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.201
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
2 more

4 mentions without citation

Structural basis for the design of potent and species-specific inhibitors of 3-hydroxy-3-methylglutaryl CoA synthases.
Pojer et al. (2006)
3 more