› 6zzn

X-ray diffraction
1.5Å resolution

Crystal structure of the cubic catalytic core of the Mycobacterium tuberculosis branched-chain alphaketoacid acyltransferase component (E2b).

Released:
DOI: 10.2210/pdb6zzn/pdb
PDB entry 6zzn coloured by chain, front view.
PDB entry 6zzn coloured by chain, side view.
PDB entry 6zzn coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Bruch EM, Vilela P, Yang L, Boyko A, Lexa-Sapart N, Raynal B, Alzari PM, Bellinzoni M
Proc Natl Acad Sci U S A 118 (2021)
PMID: 34819376

Function and Biology Details

Reaction catalysed: 
2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex Chain: A
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 24.7 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O06159 (Residues: 165-393; Coverage: 58%)
Gene names: Rv2495c, bkdC, pdhC
Sequence domains: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: F432
Unit cell:
a: 214.073Å b: 214.073Å c: 214.073Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Structures and comparison of endogenous 2-oxoglutarate and pyruvate dehydrogenase complexes from bovine kidney.
Liu et al. (2022)
5 more

1 mention without citation

Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Bruch et al. (2021)