1kv4
From Proteopedia
(New page: 200px<br /><applet load="1kv4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kv4" /> '''Solution structure of antibacterial peptide ...) |
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| - | [[Image:1kv4.gif|left|200px]]<br /><applet load="1kv4" size=" | + | [[Image:1kv4.gif|left|200px]]<br /><applet load="1kv4" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of antibacterial peptide (Moricin)'''<br /> | '''Solution structure of antibacterial peptide (Moricin)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A novel antibacterial peptide, moricin, isolated from the silkworm Bombyx | + | A novel antibacterial peptide, moricin, isolated from the silkworm Bombyx mori, consists of 42 amino acids. It is highly basic and the amino acid sequence has no significant similarity to those of other antibacterial peptides. The 20 structures of moricin in methanol have been determined from two-dimensional 1H-nuclear magnetic resonance spectroscopic data. The solution structure reveals an unique structure comprising of a long alpha-helix containing eight turns along nearly the full length of the peptide except for four N-terminal residues and six C-terminal residues. The electrostatic surface map shows that the N-terminal segment of the alpha-helix, residues 5-22, is an amphipathic alpha-helix with a clear separation of hydrophobic and hydrophilic faces, and that the C-terminal segment of the alpha-helix, residues 23-36, is a hydrophobic alpha-helix except for the negatively charged surface at the position of Asp30. The results suggest that the amphipathic N-terminal segment of the alpha-helix is mainly responsible for the increase in permeability of the membrane to kill the bacteria. |
==About this Structure== | ==About this Structure== | ||
| - | 1KV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http:// | + | 1KV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KV4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: insect immunity]] | [[Category: insect immunity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:16 2008'' |
Revision as of 11:38, 21 February 2008
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Solution structure of antibacterial peptide (Moricin)
Overview
A novel antibacterial peptide, moricin, isolated from the silkworm Bombyx mori, consists of 42 amino acids. It is highly basic and the amino acid sequence has no significant similarity to those of other antibacterial peptides. The 20 structures of moricin in methanol have been determined from two-dimensional 1H-nuclear magnetic resonance spectroscopic data. The solution structure reveals an unique structure comprising of a long alpha-helix containing eight turns along nearly the full length of the peptide except for four N-terminal residues and six C-terminal residues. The electrostatic surface map shows that the N-terminal segment of the alpha-helix, residues 5-22, is an amphipathic alpha-helix with a clear separation of hydrophobic and hydrophilic faces, and that the C-terminal segment of the alpha-helix, residues 23-36, is a hydrophobic alpha-helix except for the negatively charged surface at the position of Asp30. The results suggest that the amphipathic N-terminal segment of the alpha-helix is mainly responsible for the increase in permeability of the membrane to kill the bacteria.
About this Structure
1KV4 is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.
Reference
Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori., Hemmi H, Ishibashi J, Hara S, Yamakawa M, FEBS Lett. 2002 May 8;518(1-3):33-8. PMID:11997013
Page seeded by OCA on Thu Feb 21 13:38:16 2008
