2JNI
Spatial structure of antimicrobial peptide arenicin-2 in aqueous solution
Summary for 2JNI
| Entry DOI | 10.2210/pdb2jni/pdb |
| NMR Information | BMRB: 15115 |
| Descriptor | Arenicin-2 (1 entity in total) |
| Functional Keywords | antimicrobial, beta-sheet, antimicrobial protein |
| Biological source | Arenicola marina (lugworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 2780.37 |
| Authors | Ovchinnikova, T.V.,Shenkarev, Z.O.,Nadezhdin, K.D.,Balandin, S.V.,Zhmak, M.N.,Kudelina, I.A.,Finkina, E.I.,Kokryakov, V.N.,Arseniev, A.S. (deposition date: 2007-01-25, release date: 2007-08-07, Last modification date: 2024-11-20) |
| Primary citation | Ovchinnikova, T.V.,Shenkarev, Z.O.,Nadezhdin, K.D.,Balandin, S.V.,Zhmak, M.N.,Kudelina, I.A.,Finkina, E.I.,Kokryakov, V.N.,Arseniev, A.S. Recombinant expression, synthesis, purification, and solution structure of arenicin Biochem.Biophys.Res.Commun., 360:156-162, 2007 Cited by PubMed Abstract: Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells. PubMed: 17585874DOI: 10.1016/j.bbrc.2007.06.029 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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