Structure of the lipopeptide antibiotic tsushimycin.

@article{Bunkczi2005StructureOT,
  title={Structure of the lipopeptide antibiotic tsushimycin.},
  author={G{\'a}bor Bunk{\'o}czi and L{\'a}szl{\'o} V{\'e}rtesy and George M. Sheldrick},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2005},
  volume={61 Pt 8},
  pages={1160-4}
}
The amphomycin derivative tsushimycin has been crystallized and its structure determined at 1.0 A resolution. The asymmetric unit contains 12 molecules and with 1300 independent atoms this structure is one of the largest solved using ab initio direct methods. The antibiotic is comprised of a cyclodecapeptide core, an exocyclic amino acid and a fatty-acid residue. Its backbone adopts a saddle-like conformation that is stabilized by a Ca2+ ion bound within the peptide ring and accounts for the… CONTINUE READING

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