1kv4
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(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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Revision as of 17:47, 20 November 2007
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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
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