› 2k7v

Solution NMR

Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form

Released:
DOI: 10.2210/pdb2k7v/pdb
PDB entry 2k7v coloured by chain, ensemble of 20 models, front view.
PDB entry 2k7v coloured by chain, ensemble of 20 models, side view.
PDB entry 2k7v coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.
Stott KM, Yusof AM, Perham RN, Jones DD
Structure 17 1117-27 (2009)
PMID: 19679089

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex Chains: A, B
Molecule details ›
Chains: A, B
Length: 85 amino acids
Theoretical weight: 8.89 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P06959 (Residues: 206-293; Coverage: 13%)
Gene names: JW0111, aceF, b0115
Sequence domains: Biotin-requiring enzyme
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 30%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli

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Citations

1 review citation

A contemporary perspective on the molecular characteristics of mitochondrial autoantigens and diagnosis in primary biliary cholangitis.
Leung et al. (2016)
5 other articles