3can

X-ray diffraction
1.8Å resolution

Crystal structure of a domain of pyruvate-formate lyase-activating enzyme from Bacteroides vulgatus ATCC 8482

Released:
Entry authors: Nocek B, Hendricks R, Hatzos C, Jedrzejczak R, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-107867 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[formate-C-acetyltransferase]-activating enzyme Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 20.44 KDa
Source organism: Phocaeicola vulgatus ATCC 8482
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A6L094 (Residues: 124-302; Coverage: 59%)
Gene name: BVU_1420
Sequence domains: Radical SAM superfamily
Structure domains: pyruvate-formate lyase- activating enzyme

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 73.768Å b: 73.768Å c: 101.358Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.162 0.182
Expression system: Escherichia coli BL21(DE3)