2LG4

3D solution structure of antimicrobial peptide aurelin

Summary for 2LG4

• Entry DOI: 10.2210/pdb2lg4/pdb
• NMR Information: BMRB: 17792
• Descriptor: Aurelin (1 entity in total)
• Functional Keywords: antimicrobial protein
• Biological source: Aurelia aurita (Moon jellyfish)
• Cellular location: Secreted: Q0MWV8
• Total number of polymer chains: 1
• Total formula weight: 4313.03

Authors

Shenkarev, Z.,Altukhov, D. (deposition date: 2011-07-20, release date: 2012-07-25, Last modification date: 2024-11-27)

Primary citation

Shenkarev, Z.O.,Panteleev, P.V.,Balandin, S.V.,Gizatullina, A.K.,Altukhov, D.A.,Finkina, E.I.,Kokryakov, V.N.,Arseniev, A.S.,Ovchinnikova, T.V.
Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita.
Biochem.Biophys.Res.Commun., 429:63-69, 2012

PubMed Abstract: Aurelin is a 40-residue cationic antimicrobial peptide isolated from the mezoglea of a scyphoid jellyfish Aurelia aurita. Aurelin and its (15)N-labeled analogue were overexpressed in Escherichia coli and purified. Antimicrobial activity of the recombinant peptide was examined, and its spatial structure was studied by NMR spectroscopy. Aurelin represents a compact globule, enclosing one 3(10)-helix and two α-helical regions cross-linked by three disulfide bonds. The peptide binds to anionic lipid (POPC/DOPG, 3:1) vesicles even at physiological salt concentration, it does not interact with zwitterionic (POPC) vesicles and interacts with the DPC micelle surface with moderate affinity via two α-helical regions. Although aurelin shows structural homology to the BgK and ShK toxins of sea anemones, its surface does not possess the "functional dyad" required for the high-affinity interaction with the K(+)-channels. The obtained data permit to correlate the modest antibacterial properties and membrane activity of aurelin.

PubMed: 23137541
DOI: 10.1016/j.bbrc.2012.10.092

Experimental method

SOLUTION NMR