1x22
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1x22.gif|left|200px]]<br /><applet load="1x22" size=" | + | [[Image:1x22.gif|left|200px]]<br /><applet load="1x22" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1x22" /> | caption="1x22" /> | ||
'''Solution structure of a novel moricin analogue, an antibacterial peptide from a lepidopteran insect, Spodoptera litura'''<br /> | '''Solution structure of a novel moricin analogue, an antibacterial peptide from a lepidopteran insect, Spodoptera litura'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An antibacterial peptide was isolated from a lepidopteran insect, Spodoptera litura. The molecular mass of this peptide was determined to be | + | 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== | ==About this Structure== | ||
| - | 1X22 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1X22 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X22 OCA]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:16 2008'' |
Revision as of 13:50, 21 February 2008
|
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 Thu Feb 21 15:50:16 2008
