2G9L

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

Summary for 2G9L

• Entry DOI: 10.2210/pdb2g9l/pdb
• NMR Information: BMRB: 7065
• Descriptor: Gaegurin-4 (1 entity in total)
• Functional Keywords: amphipathic helix, antibiotic
• Cellular location: Secreted: P80398
• Total number of polymer chains: 1
• Total formula weight: 3755.49

Authors

Chi, S.-W.,Han, K.-H. (deposition date: 2006-03-06, release date: 2007-01-16, Last modification date: 2024-10-23)

Primary citation

Chi, S.-W.,Kim, J.-S.,Kim, D.-H.,Lee, S.-H.,Park, Y.-H.,Han, K.-H.
Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4
Biochem.Biophys.Res.Commun., 352:592-597, 2007

PubMed Abstract: 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.

PubMed: 17141187
DOI: 10.1016/j.bbrc.2006.11.064

Experimental method

SOLUTION NMR