6i2q

X-ray diffraction
2.15Å resolution

Crystal structure of the wild-type SucA domain of Mycobacterium smegmatis KGD (alpha-ketoglutarate decarboxylase), in complex with GarA

Released:

Function and Biology Details

Reactions catalysed:
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2)
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2)
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine
2-oxoglutarate = succinate semialdehyde + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-106379 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Multifunctional 2-oxoglutarate metabolism enzyme Chain: A
Molecule details ›
Chain: A
Length: 868 amino acids
Theoretical weight: 97.17 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0R2B1 (Residues: 361-1227; Coverage: 71%)
Gene names: MSMEG_5049, MSMEI_4922, kgd, sucA
Sequence domains:
Structure domains:
Glycogen accumulation regulator GarA Chain: B
Molecule details ›
Chain: B
Length: 115 amino acids
Theoretical weight: 12.11 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0QYG2 (Residues: 45-158; Coverage: 72%)
Gene names: MSMEG_3647, MSMEI_3561, garA
Sequence domains: FHA domain

Ligands and Environments


Cofactor: Ligand TPP 1 x TPP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2221
Unit cell:
a: 141.25Å b: 167.846Å c: 102.808Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.191
Expression system: Escherichia coli BL21(DE3)