› 2l36

Solution NMR

Solution structure of MSI-594 derived mutant peptide MSI594F5A in Lipopolysaccharide Micelles

Released:
DOI: 10.2210/pdb2l36/pdb
PDB entry 2l36 coloured by chain, ensemble of 20 models, front view.
PDB entry 2l36 coloured by chain, ensemble of 20 models, side view.
PDB entry 2l36 coloured by chain, ensemble of 20 models, top view.
Source organism: Synthetic construct
Primary publication:
Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: role of the helical hairpin conformation in outer-membrane permeabilization.
Domadia PN, Bhunia A, Ramamoorthy A, Bhattacharjya S
J Am Chem Soc 132 18417-28 (2010)
PMID: 21128620

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162862 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MSI594 Chain: A
Molecule details ›
Chain: A
Length: 24 amino acids
Theoretical weight: 2.37 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Not provided

Quick links

Citations

19 review citations

Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields.
Moretta et al. (2021)
18 more

1 mention without citation

Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control.
Datta et al. (2016)