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Crystal structures of cephaibols
Author(s) -
Bunkóczi Gábor,
Schiell Matthias,
Vértesy László,
Sheldrick George M.
Publication year - 2003
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.496
Subject(s) - crystallography , chemistry , crystal structure , molecule , hydrogen bond , crystal (programming language) , resolution (logic) , helix (gastropod) , stereochemistry , biology , ecology , organic chemistry , artificial intelligence , snail , computer science , programming language
The crystal structures of the peptaibol antibiotics cephaibol A, cephaibol B and cephaibol C have been determined at ca. 0.9 Å resolution. All three adopt a helical conformation with a sharp bend (of about 55° ) at the central hydroxyproline. All isovalines were found to possess the D configuration, superposition of all four models (there are two independent molecules in the cephaibol B structure) shows that the N ‐terminal helix is rigid and the C ‐terminus is flexible. There are differences in the hydrogen bonding patterns for the three structures that crystallize in different space groups despite relatively similar unit cell dimensions, but only in the case of cephaibol C does the packing emulate the formation of a membrane channel believed to be important for their biological function. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.