› 3hpx

X-ray diffraction
2.03Å resolution

Crystal structure of Mycobacterium tuberculosis LeuA active site domain 1-425 (truncation mutant delta:426-644)

Released:
DOI: 10.2210/pdb3hpx/pdb
PDB entry 3hpx coloured by chain, front view.
PDB entry 3hpx coloured by chain, side view.
PDB entry 3hpx coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
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-162062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-isopropylmalate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 425 amino acids
Theoretical weight: 47.54 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WQB3 (Residues: 1-425; Coverage: 66%)
Gene names: MTV025.058, Rv3710, leuA
Sequence domains: HMGL-like
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NI 2 x NI
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 48.025Å b: 70.886Å c: 70.043Å
α: 62.45° β: 81.41° γ: 70.26°
R-values:
R R work R free
0.177 0.174 0.238
Expression system: Escherichia coli

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Citations

3 review citations

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