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• W2009201439 abstract "The amphomycin derivative tsushimycin has been crystallized and its structure determined at 1.0 Å 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 Ca2+-dependence of this antibiotic class. Additional Ca2+ ions link the antibiotic molecules to dimers that enclose an empty space resembling a binding cleft. The dimers possess a large hydrophobic surface capable of interacting with the bacterial cell membrane. The antibiotic daptomycin may exhibit a similar conformation, as the amino-acid sequence is conserved at positions involved in Ca2+ binding." @default.
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• W2009201439 date "2005-07-20" @default.
• W2009201439 modified "2023-10-17" @default.
• W2009201439 title "Structure of the lipopeptide antibiotic tsushimycin" @default.
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• W2009201439 doi "https://doi.org/10.1107/s0907444905017270" @default.
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