Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan hydra
| Autor: | Jung, S., Dingley, A.J., Augustin, R., Anton-Erxleben, F., Stanisak, M., Gelhaus, C., Gutsmann, T., Hammer, M.U., Podschun, R., Bonvin, A.M.J.J., Leippe, M., Bosch, T.C.G., Grötzinger, J., NMR Spectroscopy, Sub NMR Spectroscopy |
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| Přispěvatelé: | NMR Spectroscopy, Sub NMR Spectroscopy |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Gram-negative bacteria Hydra Amino Acid Motifs Gram-Positive Bacteria Biochemistry Anti-Infective Agents Gram-Negative Bacteria Animals Humans Disulfides Molecular Biology Peptide sequence chemistry.chemical_classification biology Proteins Cell Biology Hydramacin-1 biology.organism_classification Antimicrobial Amino acid chemistry biology.protein Lernaean Hydra Antibacterial activity Bacteria Antimicrobial Cationic Peptides |
| Zdroj: | Journal of Biological Chemistry, 284(3), 1896. American Society for Biochemistry and Molecular Biology Inc. |
| ISSN: | 0021-9258 |
| Popis: | Hydramacin-1 is a novel antimicrobial protein recently discovered during investigations of the epithelial defense of the ancient metazoan Hydra. The amino acid sequence of hydramacin-1 shows no sequence homology to any known antimicrobial proteins. Determination of the solution structure revealed that hydramacin-1 possesses a disulfide bridge-stabilized alphabeta motif. This motif is the common scaffold of the knottin protein fold. The structurally closest relatives are the scorpion oxin-like superfamily. Within this superfamily hydramacin-1 establishes a new family of proteins that all share antimicrobial activity. Hydramacin-1 is potently active against Gram-positive and Gram-negative bacteria including multi-resistant human pathogenic strains. It leads to aggregation of bacteria as an initial step of its bactericidal mechanism. Aggregated cells are connected via electron-dense contacts and adopt a thorn apple-like morphology. Analysis of the hydramacin-1 structure revealed an unusual distribution of amino acid side chains on the surface. A belt of positively charged residues is sandwiched by two hydrophobic areas. Based on this characteristic surface feature and on biophysical analysis of protein-membrane interactions, we propose a model that describes the aggregation effect exhibited by hydramacin-1. |
| Databáze: | OpenAIRE |
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