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› 6trp

Solution NMR

Solution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDD

Released:
DOI: 10.2210/pdb6trp/pdb
PDB entry 6trp coloured by chain, ensemble of 20 models, front view.
PDB entry 6trp coloured by chain, ensemble of 20 models, side view.
PDB entry 6trp coloured by chain, ensemble of 20 models, top view.
Source organism: Xenorhabdus bovienii SS-2004
Primary publication:
A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase from Xenorhabdus bovienii.
Watzel J, Hacker C, Duchardt-Ferner E, Bode HB, Wöhnert J
ACS Chem Biol 15 982-989 (2020)
PMID: 32167274

Function and Biology Details

Reactions catalysed: 
L-phenylalanine + ATP + H2O = D-phenylalanine + AMP + diphosphate + H(+).
L-ornithine = D-ornithine.
2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP +diphosphate.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carrier domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 93 amino acids
Theoretical weight: 9.84 KDa
Source organism: Xenorhabdus bovienii SS-2004
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D3V3G2 (Residues: 1-33; Coverage: 1%)
  • Canonical: D3V3G3 (Residues: 3288-3321; Coverage: 1%)
Gene names: XBJ1_2151, XBJ1_2152

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 93%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Type Strains of Entomopathogenic Nematode-Symbiotic Bacterium Species, Xenorhabdus szentirmaii (EMC) and X. budapestensis (EMA), Are Exceptional Sources of Non-Ribosomal Templated, Large-Target-Spectral, Thermotolerant-Antimicrobial Peptides (by Both), and Iodinin (by EMC).
Fodor et al. (2022)
6 other articles

2 mentions without citation

Docking domain-mediated subunit interactions in natural product megasynth(et)ases.
Smith et al. (2021)
1 more