2lt8

Eurocin solution structure

spinqualitylabelsall models 2lt8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lt8 is a 1 chain structure with sequence from Aspergillus amstelodami. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DEFEU_ASPAM Publication Abstract from PubMed Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications, since they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, that have been found in different species. Here we describe a new fungal defensin, eurocin. Eurocin acts against a range of gram-positive human pathogens, but not against gram-negative bacteria. Eurocin consists of 42 amino acids, forming a cysteine-stabilized alpha/beta fold. Thermal denaturation data point shows the disulphide bridges being responsible for the stability of the fold. Eurocin does not form pores in cell membranes at physiologically relevant concentrations, it does, however, lead to limited leakage of a fluorophore from small unilamellar vesicles. Eurocin interacts with detergent micelles, and it inhibits the synthesis of cell walls by binding equimolarly to the cell wall precursor lipid II. Eurocin, a new fungal defensin: structure, lipid binding and its mode of action.,Oeemig JS, Lynggaard C, Knudsen DH, Hansen FT, Noergaard KD, Schneider T, Vad BS, Sandvang D, Nielsen LA, Neve S, Kristensen HH, Sahl HG, Otzen DE, Wimmer R J Biol Chem. 2012 Oct 23. PMID:23093408 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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