› 6ksb

X-ray diffraction
1.97Å resolution

Crystal Structure of E447A M130G Acyl-CoA Dehydrogenase FadE5 mutant from Mycobacteria smegmatis in complex with C16CoA

Released:
DOI: 10.2210/pdb6ksb/pdb
PDB entry 6ksb coloured by chain, front view.
PDB entry 6ksb coloured by chain, side view.
PDB entry 6ksb coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis
Primary publication:
Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.
Chen X, Chen J, Yan B, Zhang W, Guddat LW, Liu X, Rao Z
Proc Natl Acad Sci U S A 117 16324-16332 (2020)
PMID: 32601219

Function and Biology Details

Reactions catalysed: 
A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Long-chain-acyl-CoA + electron-transfer flavoprotein = long-chain-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Broad-specificity linear acyl-CoA dehydrogenase FadE5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 611 amino acids
Theoretical weight: 66.47 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3L887 (Residues: 1-611; Coverage: 100%)
Gene names: MSMEG_0406, MSMEI_0396, fadE5
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
3 bound ligands:
Ligand GOL 2 x GOL
Ligand PLM 2 x PLM
Ligand COA 2 x COA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21212
Unit cell:
a: 97.622Å b: 199.096Å c: 73.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.199
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Mycobacterial fatty acid catabolism is repressed by FdmR to sustain lipogenesis and virulence.
Dong et al. (2021)
5 more

1 mention without citation

Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.
Chen et al. (2020)