› 3o83

X-ray diffraction
1.9Å resolution

Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 2-(4-n-dodecyl-1,2,3-triazol-1-yl)-5'-O-[N-(2-hydroxybenzoyl)sulfamoyl]adenosine

Released:
DOI: 10.2210/pdb3o83/pdb
PDB entry 3o83 coloured by chain, front view.
PDB entry 3o83 coloured by chain, side view.
PDB entry 3o83 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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163849 (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

4 bound ligands:
Ligand IXN 2 x IXN
Ligand CA 6 x CA
Ligand MPD 1 x MPD
Ligand MRD 1 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 66.46Å b: 144.238Å c: 148.469Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

6 mentions without citation

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