What is it about?
The authors describe the atomic structure of bergofungin A, which has been determined with X-ray diffraction from a tiny single crystal of this natural antibiotic peptide.
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Why is it important?
This work expands the limited set of known structures of peptaibols, which constitute a large superfamily of natural antibiotic peptides like the well characterised alamethicin.
Perspectives
X-ray crystallography combined with other structural methods like NMR (in solution and solid state) may provide a molecular mechanism for the function of peptaibols that form hydrophilic channels in biological membranes.
Dr. Kyriacos Petratos
IMBB-FoRTH
Read the Original
This page is a summary of: A natural, single-residue substitution yields a less active peptaibiotic: the structure of bergofungin A at atomic resolution, Acta Crystallographica Section F Structural Biology Communications, January 2017, International Union of Crystallography,
DOI: 10.1107/s2053230x17001236.
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