2LR5
1H chemical shift assignments for micasin
Summary for 2LR5
| Entry DOI | 10.2210/pdb2lr5/pdb |
| NMR Information | BMRB: 18347 |
| Descriptor | micasin (1 entity in total) |
| Functional Keywords | antimicrobial protein |
| Biological source | Arthroderma otae (Microsporum canis) |
| Total number of polymer chains | 1 |
| Total formula weight | 4067.70 |
| Authors | Harvey, P.J.,Craik, D.J.,Zhu, S. (deposition date: 2012-03-22, release date: 2012-06-27, Last modification date: 2024-11-13) |
| Primary citation | Zhu, S.,Gao, B.,Harvey, P.J.,Craik, D.J. Dermatophytic defensin with antiinfective potential Proc.Natl.Acad.Sci.USA, 109:8495-8500, 2012 Cited by PubMed Abstract: Fungi are a newly emerging source of peptide antibiotics with therapeutic potential. Here, we report 17 new fungal defensin-like peptide (fDLP) genes and the detailed characterization of a corresponding synthetic fDLP (micasin) from a dermatophyte in terms of its structure, activity and therapeutic potential. NMR analysis showed that synthetic micasin adopts a "hallmark" cysteine-stabilized α-helical and β-sheet fold. It was active on both gram-positive and gram-negative bacteria, and importantly it killed two clinical isolates of methicillin-resistant Staphylococcus aureus and the opportunistic pathogen Pseudomonas aeruginosa at low micromolar concentrations. Micasin killed approximately 100% of treated bacteria within 3 h through a membrane nondisruptive mechanism of action, and showed extremely low hemolysis and high serum stability. Consistent with these functional properties, micasin increases survival in mice infected by the pathogenic bacteria in a peritonitis model. Our work represents a valuable approach to explore novel peptide antibiotics from a large resource of fungal genomes. PubMed: 22586077DOI: 10.1073/pnas.1201263109 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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