› 6h05

Electron Microscopy
2.9Å resolution

Cryo-electron microscopic structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate (2-oxoglutarate) dehydrogenase complex [residues 218-453]

Released:
DOI: 10.2210/pdb6h05/pdb
PDB entry 6h05 coloured by chain, front view.
PDB entry 6h05 coloured by chain, side view.
PDB entry 6h05 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: Implications for the overall hKGDHc structure.
Nagy B, Polak M, Ozohanics O, Zambo Z, Szabo E, Hubert A, Jordan F, Novaček J, Adam-Vizi V, Ambrus A
Biochim Biophys Acta Gen Subj 1865 129889 (2021)
PMID: 33684457
Related structures: EMD-0108

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 analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153268 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 426 amino acids
Theoretical weight: 45.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36957 (Residues: 68-453; Coverage: 85%)
Gene names: DLST, DLTS
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-0108
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Lipoamide dehydrogenase (LADH) deficiency: medical perspectives of the structural and functional characterization of LADH and its pathogenic variants.
Szabó et al. (2023)
1 more

17 mentions without citation

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.
Lu et al. (2016)
16 more