› 1c4t

X-ray diffraction
3Å resolution

CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

Released:
DOI: 10.2210/pdb1c4t/pdb
PDB entry 1c4t coloured by chain, front view.
PDB entry 1c4t coloured by chain, side view.
PDB entry 1c4t coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase.
Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, Hackert ML
Protein Sci 9 37-48 (2000)
PMID: 10739245

Function and Biology Details

Reaction catalysed: 
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 233 amino acids
Theoretical weight: 26.11 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AFG6 (Residues: 173-405; Coverage: 58%)
Gene names: JW0716, b0727, sucB
Sequence domains: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
Structure domains: Chloramphenicol acetyltransferase-like domain

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 112.175Å b: 112.175Å c: 134.417Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.257 0.257 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Toward an Understanding of the Structural and Mechanistic Aspects of Protein-Protein Interactions in 2-Oxoacid Dehydrogenase Complexes.
Nemeria et al. (2021)
15 other articles

6 mentions without citation

Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex.
Wang et al. (2014)
5 more