1x22
From Proteopedia
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| - | [[Image:1x22.gif|left|200px]] | + | [[Image:1x22.gif|left|200px]] |
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| - | '''Solution structure of a novel moricin analogue, an antibacterial peptide from a lepidopteran insect, Spodoptera litura''' | + | {{Structure |
| + | |PDB= 1x22 |SIZE=350|CAPTION= <scene name='initialview01'>1x22</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of a novel moricin analogue, an antibacterial peptide from a lepidopteran insect, Spodoptera litura''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1X22 is a [ | + | 1X22 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16115804 16115804] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Asaoka, A.]] | [[Category: Asaoka, A.]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:04:12 2008'' |
Revision as of 13:04, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 15:04:12 2008
