› 3u6w

X-ray diffraction
2.21Å resolution

Truncated M. tuberculosis LeuA (1-425) complexed with KIV

Released:
DOI: 10.2210/pdb3u6w/pdb
PDB entry 3u6w coloured by chain, front view.
PDB entry 3u6w coloured by chain, side view.
PDB entry 3u6w 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: 427 amino acids
Theoretical weight: 47.67 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

3 bound ligands:
Ligand MN 2 x MN
Ligand KIV 2 x KIV
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: 47.715Å b: 70.566Å c: 69.879Å
α: 62.29° β: 81.26° γ: 70.16°
R-values:
R R work R free
0.228 0.225 0.298
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

2 mentions without citation

Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.
Amorim Franco et al. (2017)
1 more