› 2mcu

Solid-state NMR

Solid-state NMR structure of piscidin 1 in aligned 3:1 phosphatidylcholine/phosphoglycerol lipid bilayers

Released:
DOI: 10.2210/pdb2mcu/pdb
PDB entry 2mcu coloured by chain, ensemble of 10 models, front view.
PDB entry 2mcu coloured by chain, ensemble of 10 models, side view.
PDB entry 2mcu coloured by chain, ensemble of 10 models, top view.
Source organism: Morone saxatilis
Primary publication:
High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion.
Perrin BS, Tian Y, Fu R, Grant CV, Chekmenev EY, Wieczorek WE, Dao AE, Hayden RM, Burzynski CM, Venable RM, Sharma M, Opella SJ, Pastor RW, Cotten ML
J Am Chem Soc 136 3491-504 (2014)
PMID: 24410116

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Moronecidin Chain: A
Molecule details ›
Chain: A
Length: 23 amino acids
Theoretical weight: 2.58 KDa
Source organism: Morone saxatilis
Expression system: Not provided
UniProt:
  • Canonical: Q8UUG0 (Residues: 23-44; Coverage: 39%)
Sequence domains: Pleurocidin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 8%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

10 review citations

Antimicrobial peptides in 2014.
Wang et al. (2015)
9 more

2 mentions without citation

High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion.
Perrin et al. (2014)
1 more