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2M8V

Solution Structure and Activity Study of Bovicin HJ50, a Particular Type AII Lantibiotic

Summary for 2M8V
Entry DOI10.2210/pdb2m8v/pdb
NMR InformationBMRB: 19275
DescriptorBovA (1 entity in total)
Functional Keywordslantibiotic, antibiotic
Biological sourceStreptococcus equinus
Total number of polymer chains1
Total formula weight3440.09
Authors
Zhang, J.,Feng, Y.,Wang, J.,Zhong, J. (deposition date: 2013-05-29, release date: 2014-05-21, Last modification date: 2024-07-10)
Primary citationZhang, J.,Feng, Y.,Teng, K.,Lin, Y.,Gao, Y.,Wang, J.,Zhong, J.
Type AII lantibiotic bovicin HJ50 with a rare disulfide bond: structure, structure-activity relationships and mode of action.
Biochem.J., 461:497-508, 2014
Cited by
PubMed Abstract: Lantibiotics are ribosomally synthesized antimicrobial peptides containing unusual amino acids. As promising alternatives to conventional antibiotics, they have a high potential for alleviating the problem of emergent antibiotic resistance, with possible applications in many industries that have antibacterial demand. Bovicin HJ50 is a type AII lantibiotic, the largest group of lantibiotics, comprising a linear N-terminal region and a globular C-terminal region. Interestingly, bovicin H50 has a disulfide bond that is rare in this group. Owing 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. In the present study, 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, whereas varied rigidities were observed in the different rings with the conserved ring A being the most rigid. The charged residues Lys¹¹, Asp¹² and Lys³⁰, 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.
PubMed: 24814218
DOI: 10.1042/BJ20131524
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-11-06公开中

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