Structure of thermolysin cleaved microcin J25: extreme stability of a two-chain antimicrobial peptide devoid of covalent links.

@article{Rosengren2004StructureOT,
  title={Structure of thermolysin cleaved microcin J25: extreme stability of a two-chain antimicrobial peptide devoid of covalent links.},
  author={K Johan Rosengren and Alain Blond and Carlos Afonso and J C Tabet and Sylvie Rebuffat and David J. Craik},
  journal={Biochemistry},
  year={2004},
  volume={43 16},
  pages={4696-702}
}
The structure of a two-chain peptide formed by the treatment of the potent antimicrobial peptide microcin J25 (MccJ25) with thermolysin has been characterized by NMR spectroscopy and mass spectrometry. The native peptide is 21 amino acids in size and has the remarkable structural feature of a ring formed by linkage of the side chain of Glu8 to the N-terminus that is threaded by the C-terminal tail of the peptide. Thermolysin cleaves the peptide at the Phe10-Val11 amide bond, but the threading… CONTINUE READING

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