Structural highlights
FunctionPublication Abstract from PubMedLantibiotics are ribosomally synthesized antimicrobial peptides containing unusual amino acids. As promising alternatives to conventional antibiotics, they have high potential for alleviating the problem of emergent antibiotic resistance, with potential applications in many industries that have antibacterial demand. Bovicin HJ50 is a type AII lantibiotic, the largest group of lantibiotics, comprised of a linear N-terminal region and a globular C-terminal region. Interestingly, bovicin H50 has a disulfide bond that is rare in this group. Due to limited information about the spatial structures of type AII lantibiotics, the functional regions of this type and the role of the disulfide bond are still unknown. Here we resolved the solution structure of bovicin HJ50 using NMR spectroscopy. This is the first spatial structure of a type AII lantibiotic. Bovicin HJ50 exhibited high flexibility in aqueous solution, while varied rigidities were observed in the different rings with the conserved ring A being the most rigid. The charged residues K11, D12 and K30, as well as the essential disulfide bond were critical for antimicrobial activity. Importantly, bovicin HJ50 showed not only peptidoglycan precursor lipid II-binding ability but also pore-forming activity, which is significantly different from other bacteriostatic type AII lantibiotics, suggesting a novel antimicrobial mechanism. Type AII Lantibiotic Bovicin HJ50 with a Rare Disulfide Bond: Structure, Structure-Activity Relationships and Mode of Action.,Zhang J, Feng Y, Teng K, Lin Y, Gao Y, Wang J, Zhong J Biochem J. 2014 May 12. PMID:24814218[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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