1zrw | pdb_00001zrw

solution structure of spinigerin in H20/TFE 10%

spinqualitylabelsall models 1zrw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zrw is a 1 chain structure with sequence from Pseudacanthotermes spiniger. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPING_PSEUS Active against Gram-positive bacteria B.megaterium and M.luteus, Gram-negative bacteria E.coli SBS363 and D22, K.pneumoniae, S.typhimurium and P.aeruginosa, yeast C.albicans and filamentous fungi F.culmorum, N.crassa, N.hematococca and T.viridae. Inactive against Gram-positive bacteria B.subtilis, S.pyogenes, B.thuringiensis and S.aureus, Gram-negative bacteria E.cloacae and E.carotovora and filamentous fungus B.bassiana. Publication Abstract from PubMed Stomoxyn and spinigerin belong to the class of linear cysteine-free insect antimicrobial peptides that kill a range of microorganisms, parasites, and some viruses but without any lytic activity against mammalian erythrocytes. Stomoxyn is localized in the gut epithelium of the nonvector stable fly that is sympatric with the trypanosome vector tsetse fly. Spinigerin is stored and secreted by hemocytes from the fungus-growing termite. The structure of synthetic stomoxyn and spinigerin in aqueous solution and in TFE/water mixtures was analyzed by CD and NMR spectroscopy combined with molecular modeling calculations. Stomoxyn and spinigerin adopt a flexible random coil structure in water while both assume a stable helical structure in the presence of TFE. In 50% TFE, the structure of stomoxyn is typical of cecropins, including an amphipathic helix at the N-terminus and a hydrophobic C-terminus with helical features that probably fold in a helical conformation at higher TFE concentration. In contrast to stomoxyn, spinigerin acquires very rapidly a helical conformation. In 10% TFE the helix is highly bent and the structure is poorly defined. In 50% TFE, the helical structure is well defined all along its sequence, and the slightly bent alpha-helix displays an amphiphilic character, as observed for magainin 2. The structural similarities between stomoxyn and cecropin A from Hyalophora cecropia and between spinigerin and magainin 2 suggest a similar mode of action on the bacterial membranes of both pairs of peptides. Our results also confirm that TFE induces helix formation and propagation for amino acids showing helical propensity in water but also enhances the helix propagation propensity of nonpolar beta-branched residues. Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation.,Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F Biopolymers. 2006 Feb 5;81(2):92-103. PMID:16170803 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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