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1x22
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(New page: 200px<br /><applet load="1x22" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x22" /> '''Solution structure of a novel moricin analog...)
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Revision as of 23:10, 24 November 2007
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Solution structure of a novel moricin analogue, an antibacterial peptide from a lepidopteran insect, Spodoptera litura
Overview
An antibacterial peptide was isolated from a lepidopteran insect, Spodoptera litura. The molecular mass of this peptide was determined to be, 4489.55 by matrix assisted laser desorption/ionization-time of flight mass, (MALDI-TOF MS) spectrometry. The peptide consists of 42 amino acids and, the sequence has 69-98% identity to those of moricin-related peptides, antibacterial peptides from lepidopetran insects. Thus, the peptide was, designated S. litura (Sl) moricin. Sl moricin showed a broad antibacterial, spectrum against Gram-positive and negative bacteria. Sl moricin gene was, inducible by bacterial injection and expressed tissue-specifically in the, fat body and hemocytes. Furthermore, the solution structure of Sl moricin, was determined by two-dimensional (2D) 1H-nuclear magnetic resonance (NMR), spectroscopy and hybrid distance geometry-simulated annealing calculation., The tertiary structure revealed a long alpha-helix containing eight turns, along nearly the full length of the peptide like that of moricin, confirming that Sl moricin is a new moricin-like antibacterial peptide., These results suggest that moricin is present not only in B. mori but also, in other lepidopteran insects forming a gene family.
About this Structure
1X22 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Isolation, gene expression and solution structure of a novel moricin analogue, antibacterial peptide from a lepidopteran insect, Spodoptera litura., Oizumi Y, Hemmi H, Minami M, Asaoka A, Yamakawa M, Biochim Biophys Acta. 2005 Aug 31;1752(1):83-92. PMID:16115804
Page seeded by OCA on Sun Nov 25 01:18:03 2007
