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Silvia C Bobeica1, Lingyang Zhu2, Jeella Z Acedo1

  • 1Department of Chemistry and Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign 600 South Mathews Avenue Urbana Illinois 61801 USA vddonk@illinois.edu +1-217-244-8533 +1-217-244-5360.

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This study reveals how precursor peptide sequences dictate lanthipeptide structures, impacting cyclization patterns and stereochemistry. Understanding these molecular determinants is key for developing novel antibiotics and therapeutic agents.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Lanthipeptides are ribosomally synthesized peptides with unique thioether crosslinks from post-translational modifications.
  • The cyclization process determining lanthipeptide ring patterns and stereochemistry remains poorly understood, with recent evidence pointing to precursor peptide sequences.

Purpose of the Study:

  • To elucidate the molecular determinants governing lanthipeptide cyclization.
  • To present the first 3D structures of five prochlorosins and the enterococcal cytolysin subunits.
  • To investigate how substrate sequences influence cyclization patterns and stereochemistry.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy was used to determine the three-dimensional structures of seven lanthipeptides.
  • Structural analysis focused on prochlorosins and the subunits of enterococcal cytolysin.

Main Results:

  • Determined the 3D structures of prochlorosins 1.1, 2.1, 2.8, 2.10, and 2.11, providing insights into their cyclization patterns.
  • Revealed that prochlorosin substrate sequences dictate cyclization patterns.
  • Showed that enterococcal cytolysin subunits possess extensive helical structures, potentially explaining pore-forming activity.

Conclusions:

  • Peptide sequence is a critical determinant of lanthipeptide cyclization pattern and stereochemistry.
  • Prochlorosin structures offer potential starting points for library generation.
  • Enterococcal cytolysin's helical structure suggests a mechanism for membrane pore formation and virulence.