2K35
Hydramacin-1: Structure and antibacterial activity of a peptide from the basal metazoan Hydra
Summary for 2K35
| Entry DOI | 10.2210/pdb2k35/pdb |
| Descriptor | hydramacin-1 (1 entity in total) |
| Functional Keywords | antimicrobial protein |
| Biological source | Hydra |
| Total number of polymer chains | 1 |
| Total formula weight | 7029.12 |
| Authors | Jung, S.,Dingley, A.J.,Stanisak, M.,Gelhaus, C.,Bosch, T.,Podschun, R.,Leippe, M.,Gr tzinger, J. (deposition date: 2008-04-22, release date: 2008-11-18, Last modification date: 2024-10-16) |
| Primary citation | Jung, S.,Dingley, A.J.,Augustin, R.,Anton-Erxleben, F.,Stanisak, M.,Gelhaus, C.,Gutsmann, T.,Hammer, M.U.,Podschun, R.,Bonvin, A.M.,Leippe, M.,Bosch, T.C.,Grotzinger, J. Hydramacin-1, structure and antibacterial activity of a protein from the Basal metazoan hydra. J.Biol.Chem., 284:1896-1905, 2009 Cited by PubMed Abstract: 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. PubMed: 19019828DOI: 10.1074/jbc.M804713200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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