› 3rmj

X-ray diffraction
1.95Å resolution

Crystal structure of truncated alpha-Isopropylmalate Synthase from Neisseria meningitidis

Released:
DOI: 10.2210/pdb3rmj/pdb
PDB entry 3rmj coloured by chain, front view.
PDB entry 3rmj coloured by chain, side view.
PDB entry 3rmj coloured by chain, top view.
Source organism: Neisseria meningitidis serogroup B
Primary publication:
Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding.
Huisman FH, Koon N, Bulloch EM, Baker HM, Baker EN, Squire CJ, Parker EJ
Biochemistry 51 2289-97 (2012)
PMID: 22352945

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-isopropylmalate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 370 amino acids
Theoretical weight: 39.98 KDa
Source organism: Neisseria meningitidis serogroup B
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JZG1 (Residues: 1-364; Coverage: 70%)
Gene names: NMB1070, leuA
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand MN 2 x MN
Ligand MG 2 x MG
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 46.296Å b: 103.581Å c: 129.937Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.191
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Engineering Allostery into Proteins.
Gorman et al. (2019)
2 more

3 mentions without citation

Changing substrate specificity and iteration of amino acid chain elongation in glucosinolate biosynthesis through targeted mutagenesis of Arabidopsis methylthioalkylmalate synthase 1.
Petersen et al. (2019)
2 more