X-ray diffraction
2.1Å resolution

Crystal structure of N-terminal domain of putative 2-isopropylmalate synthase from Listeria monocytogenes

Entry authors: Ramagopal UA, Toro R, Gilmore M, Hu S, Maletic M, Rodgers L, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2-isopropylmalate synthase Chain: X
Molecule details ›
Chain: X
Length: 293 amino acids
Theoretical weight: 32.69 KDa
Source organism: Listeria monocytogenes serotype 4b str. F2365
Expression system: Escherichia coli
  • Canonical: Q71Y35 (Residues: 2-283; Coverage: 55%)
Gene names: LMOf2365_2010, leuA
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3121
Unit cell:
a: 72.063Å b: 72.063Å c: 106.622Å
α: 90° β: 90° γ: 120°
R R work R free
0.196 0.194 0.245
Expression system: Escherichia coli