2JSB

Solution structure of arenicin-1

Summary for 2JSB

• Entry DOI: 10.2210/pdb2jsb/pdb
• NMR Information: BMRB: 15359
• Descriptor: Arenicin-1 (1 entity in total)
• Functional Keywords: arenicin, arenicin-1, antimicrobial, arenicola marina, poreforming, antimicrobial protein
• Biological source: Arenicola marina (Lugworm)
• Total number of polymer chains: 1
• Total formula weight: 2766.35

Authors

Jakovkin, I.B.,Hecht, O.,Gelhaus, C.,Krasnosdembskaya, A.D.,Fedders, H.,Leippe, M.,Groetzinger, J. (deposition date: 2007-07-02, release date: 2008-02-05, Last modification date: 2020-02-19)

Primary citation

Andra, J.,Jakovkin, I.,Grotzinger, J.,Hecht, O.,Krasnosdembskaya, A.D.,Goldmann, T.,Gutsmann, T.,Leippe, M.
Structure and mode of action of the antimicrobial peptide arenicin
Biochem.J., 410:113-122, 2008

PubMed Abstract: The solution structure and the mode of action of arenicin isoform 1, an antimicrobial peptide with a unique 18-residue loop structure, from the lugworm Arenicola marina were elucidated here. Arenicin folds into a two-stranded antiparallel beta-sheet. It exhibits high antibacterial activity at 37 and 4 degrees C against Gram-negative bacteria, including polymyxin B-resistant Proteus mirabilis. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity. Arenicin-induced current fluctuations in planar lipid bilayers correspond to the formation of short-lived heterogeneously structured lesions. Our results strongly suggest that membrane interaction plays a pivotal role in the antibacterial activity of arenicin.

PubMed: 17935487
DOI: 10.1042/BJ20071051

Experimental method

SOLUTION NMR