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The 3D Solution Structure of Thurincin H, a Bacteriocin with Four Sulfur to α-Carbon Crosslinks


  • We thank Dr. Randy Whittal, Jing Zheng, and Bela Reiz for performing the mass spectrometry analysis. We thank Mark Miskolzie for advice regarding NMR experiments and data analysis. We thank Dr. Leah Martin-Visscher and Dr. Pascal Mercier for their assistance with CYANA. This research was supported by the Alberta Scholarship Programs (to C.S.S.), the Natural Sciences and Engineering Research Council of Canada (NSERC), the Canada Research Chair in Bioorganic and Medicinal Chemistry, the Alberta Heritage Foundation for Medical Research (AHFMR), and the United States Department of Agriculture—National Integrated Food Safety Initiative (USDA-NIFSI) Grant no. 2008-51110-0688.


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Problem solved: Thurincin H is an antimicrobial peptide with suspected post-translational modifications. MS/MS sequencing identified the residues that were modified, and NMR spectroscopic studies in solution led to the 3D structure of thurincin H, which features four S[BOND]Cα thioether crosslinks (yellow in schematic representation). This structure may be representative of several other bacteriocins with identical masses.