2g9l

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The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction

Overview

We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4.

About this Structure

2G9L is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4., Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH, Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. Epub 2006 Nov 27. PMID:17141187

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