› 3o82

X-ray diffraction
2.7Å resolution

Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl] adenosine

Released:
DOI: 10.2210/pdb3o82/pdb
PDB entry 3o82 coloured by chain, front view.
PDB entry 3o82 coloured by chain, side view.
PDB entry 3o82 coloured by chain, top view.
Source organism: Acinetobacter baumannii AB900
Primary publication:
Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.
Drake EJ, Duckworth BP, Neres J, Aldrich CC, Gulick AM
Biochemistry 49 9292-305 (2010)
PMID: 20853905

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-163847 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide arylation enzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 544 amino acids
Theoretical weight: 60.87 KDa
Source organism: Acinetobacter baumannii AB900
Expression system: Escherichia coli BL21(DE3)
Structure domains: N-terminal domain of ligase-like

Ligands and Environments

2 bound ligands:
Ligand HP8 2 x HP8
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 65.447Å b: 145.259Å c: 149.063Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Microbial siderophores: a mini review.
Saha et al. (2013)
7 more

7 mentions without citation

Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy.
Lamb AL. (2015)
6 more