› 7kq4

X-ray diffraction
2.26Å resolution

Structure of isethionate sulfite-lyase from Bilophila wadsworthia with glycerol bound

Released:
DOI: 10.2210/pdb7kq4/pdb
PDB entry 7kq4 coloured by chain, front view.
PDB entry 7kq4 coloured by chain, side view.
PDB entry 7kq4 coloured by chain, top view.
Source organism: Bilophila wadsworthia 3_1_6
Primary publication:
Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.
Dawson CD, Irwin SM, Backman LRF, Le C, Wang JX, Vennelakanti V, Yang Z, Kulik HJ, Drennan CL, Balskus EP
Cell Chem Biol 28 1333-1346.e7 (2021)
PMID: 33773110

Function and Biology Details

Reaction catalysed: 
Isethionate = acetaldehyde + sulfite
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isethionate sulfite-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 830 amino acids
Theoretical weight: 94.08 KDa
Source organism: Bilophila wadsworthia 3_1_6
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E5Y378 (Residues: 1-830; Coverage: 100%)
Gene names: HMPREF0179_00639, iseG, islA
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21212
Unit cell:
a: 120.064Å b: 132.962Å c: 107.934Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.198
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Energy Conservation in Fermentations of Anaerobic Bacteria.
Buckel W. (2021)
1 more

2 mentions without citation

Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.
Dawson et al. (2021)
1 more