› 3mi3

X-ray diffraction
2.38Å resolution

Homocitrate Synthase Lys4 bound to Lysine

Released:
DOI: 10.2210/pdb3mi3/pdb
PDB entry 3mi3 coloured by chain, front view.
PDB entry 3mi3 coloured by chain, side view.
PDB entry 3mi3 coloured by chain, top view.
Source organism: Schizosaccharomyces pombe
Primary publication:
Structural basis for L-lysine feedback inhibition of homocitrate synthase.
Bulfer SL, Scott EM, Pillus L, Trievel RC
J Biol Chem 285 10446-53 (2010)
PMID: 20089861

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + 2-oxoglutarate = (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homocitrate synthase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 423 amino acids
Theoretical weight: 46.75 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y823 (Residues: 1-418; Coverage: 100%)
Gene names: SPBC1105.02c, lys4
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand LYS 2 x LYS
Ligand ZN 2 x ZN
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P62
Unit cell:
a: 135.637Å b: 135.637Å c: 122.928Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.17 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Toward biotechnological production of adipic acid and precursors from biorenewables.
Polen et al. (2013)
3 more

1 mention without citation

High-Level Production of Lysine in the Yeast Saccharomyces cerevisiae by Rational Design of Homocitrate Synthase.
Isogai et al. (2021)