› 2n5y

Solution NMR

Solution NMR structure of octyl-tridecaptin A1 in DPC micelles containing Gram-negative lipid II

Released:
DOI: 10.2210/pdb2n5y/pdb
PDB entry 2n5y coloured by chain, ensemble of 20 models, front view.
PDB entry 2n5y coloured by chain, ensemble of 20 models, side view.
PDB entry 2n5y coloured by chain, ensemble of 20 models, top view.
Source organism: Synthetic construct
Primary publication:
Antimicrobial lipopeptide tridecaptin A1 selectively binds to Gram-negative lipid II.
Cochrane SA, Findlay B, Bakhtiary A, Acedo JZ, Rodriguez-Lopez EM, Mercier P, Vederas JC
Proc Natl Acad Sci U S A 113 11561-11566 (2016)
PMID: 27688760

Function and Biology Details

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-163047 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Octyl-tridecaptin A1 Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.52 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
3 modified residues:
Ligand DSN 1 x DSN
Ligand DTR 1 x DTR
Ligand DAB 1 x DAB

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 49%
Refinement method: distance geometry
Expression system: Not provided

Quick links

Citations

16 review citations

Antimicrobial peptides: Promising alternatives in the post feeding antibiotic era.
Wang et al. (2019)
15 more

2 mentions without citation

The tridecaptins: non-ribosomal peptides that selectively target Gram-negative bacteria.
Bann et al. (2021)
1 more