1z64

NMR Solution Structure of Pleurocidin in DPC Micelles

spinqualitylabelsall models 1z64 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1z64 is a 1 chain structure with sequence from Pseudopleuronectes americanus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 11 models Ligands: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLE1_PSEAM Antimicrobial peptide with potent activity against Gram-positive and Gram-negative bacteria. Activity against E.coli and B.subtilis. Weaker activity against L.mucor, s.marcescens and P.aeruginosa. May play a role in innate host defense. Publication Abstract from PubMed 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. Structural characterization of the antimicrobial peptide pleurocidin from winter flounder.,Syvitski RT, Burton I, Mattatall NR, Douglas SE, Jakeman DL Biochemistry. 2005 May 17;44(19):7282-93. PMID:15882067 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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