7f2r

X-ray diffraction
1.95Å resolution

Crystal structure of VinK-VinL covalent complex formed with a pantetheineamide cross-linking probe

Released:
Source organism: Streptomyces halstedii
Primary publication:
Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe.
Acta Crystallogr F Struct Biol Commun 77 294-302 (2021)
PMID: 34473106

Function and Biology Details

Reaction catalysed:
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-181172 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
[acyl-carrier-protein] S-malonyltransferase Chains: A, C
Molecule details ›
Chains: A, C
Length: 328 amino acids
Theoretical weight: 36.27 KDa
Source organism: Streptomyces halstedii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q76KY5 (Residues: 1-327; Coverage: 100%)
Gene name: vinK
Sequence domains: VinK acyltransferase small domain
Carrier domain-containing protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 85 amino acids
Theoretical weight: 9.9 KDa
Source organism: Streptomyces halstedii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q76KY4 (Residues: 1-82; Coverage: 100%)
Gene name: vinL
Sequence domains: Phosphopantetheine attachment site

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 44.282Å b: 148.224Å c: 68.791Å
α: 90° β: 91.08° γ: 90°
R-values:
R R work R free
0.196 0.193 0.241
Expression system: Escherichia coli BL21(DE3)