› 7ly4

Electron Microscopy
3.8Å resolution

Cryo-EM structure of the elongation module of the bacillamide NRPS, BmdB, in complex with the oxidase, BmdC

Released:
DOI: 10.2210/pdb7ly4/pdb
PDB entry 7ly4 coloured by chain, front view.
PDB entry 7ly4 coloured by chain, side view.
PDB entry 7ly4 coloured by chain, top view.
Source organism: Thermoactinomyces vulgaris
Primary publication:
Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module.
Fortinez CM, Bloudoff K, Harrigan C, Sharon I, Strauss M, Schmeing TM
OpenAccess logo Nat Commun 13 548 (2022)
PMID: 35087027
Related structures: EMD-23587

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-168466 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
BmdC, Oxidase Chains: A, D
Molecule details ›
Chains: A, D
Length: 336 amino acids
Theoretical weight: 38.18 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Escherichia coli
BmdB, bacillamide NRPS Chain: E
Molecule details ›
Chain: E
Length: 1028 amino acids
Theoretical weight: 117.37 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Escherichia coli

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-23587
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Bacillamide F, Extracted from Marine Bacillus atrophaeus C89, Preliminary Effects on Leukemia Cell Lines.
Zhang et al. (2022)
3 more

2 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
1 more