6HN9
Nicomicin-1 -- Novel antimicrobial peptides from the Arctic polychaeta Nicomache minor provide new molecular insight into biological role of the BRICHOS domain
Summary for 6HN9
| Entry DOI | 10.2210/pdb6hn9/pdb |
| NMR Information | BMRB: 34313 |
| Descriptor | Nicomicin-1 (1 entity in total) |
| Functional Keywords | protein, antimicrobial protein |
| Biological source | Nicomache minor |
| Total number of polymer chains | 1 |
| Total formula weight | 3544.13 |
| Authors | Panteleev, P.V.,Tsarev, A.V.,Bolosov, I.A.,Paramonov, A.S.,Marggraf, M.B.,Sychev, S.V.,Shenkarev, Z.O.,Ovchinnikova, T.V. (deposition date: 2018-09-14, release date: 2018-11-07, Last modification date: 2024-11-06) |
| Primary citation | Panteleev, P.V.,Tsarev, A.V.,Bolosov, I.A.,Paramonov, A.S.,Marggraf, M.B.,Sychev, S.V.,Shenkarev, Z.O.,Ovchinnikova, T.V. Novel Antimicrobial Peptides from the Arctic PolychaetaNicomache minorProvide New Molecular Insight into Biological Role of the BRICHOS Domain. Mar Drugs, 16:-, 2018 Cited by PubMed Abstract: Endogenous antimicrobial peptides (AMPs) are among the earliest molecular factors in the evolution of animal innate immunity. In this study, novel AMPs named nicomicins were identified in the small marine polychaeta in the Maldanidae family. Full-length mRNA sequences encoded 239-residue prepropeptides consisting of a putative signal sequence region, the BRICHOS domain within an acidic proregion, and 33-residue mature cationic peptides. Nicomicin-1 was expressed in the bacterial system, and its spatial structure was analyzed by circular dichroism and nuclear magnetic resonance spectroscopy. Nicomicins are unique among polychaeta AMPs scaffolds, combining an amphipathic -terminal α-helix and -terminal extended part with a six-residue loop stabilized by a disulfide bridge. This structural arrangement resembles the Rana-box motif observed in the α-helical host-defense peptides isolated from frog skin. Nicomicin-1 exhibited strong in vitro antimicrobial activity against Gram-positive bacteria at submicromolar concentrations. The main mechanism of nicomicin-1 action is based on membrane damage but not on the inhibition of bacterial translation. The peptide possessed cytotoxicity against cancer and normal adherent cells as well as toward human erythrocytes. PubMed: 30360541DOI: 10.3390/md16110401 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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