1Z64
NMR Solution Structure of Pleurocidin in DPC Micelles
Summary for 1Z64
| Entry DOI | 10.2210/pdb1z64/pdb |
| Descriptor | Pleruocidin (1 entity in total) |
| Functional Keywords | helix; micelle, antimicrobial protein |
| Biological source | Pseudopleuronectes americanus (winter flounder) |
| Cellular location | Secreted: P81941 |
| Total number of polymer chains | 1 |
| Total formula weight | 2716.19 |
| Authors | Syvitski, R.T.,Burton, I.,Mattatall, N.R.,Douglas, S.E.,Jakeman, D.L. (deposition date: 2005-03-21, release date: 2005-04-12, Last modification date: 2024-11-06) |
| Primary citation | Syvitski, R.T.,Burton, I.,Mattatall, N.R.,Douglas, S.E.,Jakeman, D.L. Structural characterization of the antimicrobial peptide pleurocidin from winter flounder. Biochemistry, 44:7282-7293, 2005 Cited by PubMed Abstract: Pleurocidin is an antimicrobial peptide that was isolated from the mucus membranes of winter flounder (Pseudopleuronectes americanus) and contributes to the initial stages of defense against bacterial infection. From NMR structural studies with the uniformly (15)N-labeled peptide, a structure of pleurocidin was determined to be in a random coil conformation in aqueous solution whereas it assumes an alpha-helical structure in TFE and in dodecylphosphocholine (DPC) micelles. From (15)N relaxation studies, the helix is a rigid structure in the membrane-mimicking environment. Strong NOESY cross-peaks from the pleurocidin to the aliphatic chain on DPC confirm that pleurocidin is contained within the DPC micelle and not associated with the surface of the micelle. From diffusion studies it was determined that each micelle contains at least two pleurocidin molecules. PubMed: 15882067DOI: 10.1021/bi0504005 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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