title: The crystal structure of Z-Aib-Gly-Aib-Leu-Aib-OtBu, the synthetic, protected N-terminal pentapeptide of trichotoxin.
abstract: Z-Aib-Gly-Aib-Leu-Aib-OtBu, the alpha-aminoisobutyric acid (Aib)-containing N-terminal pentapeptide of the antibiotic trichotoxin, has been studied by x-ray crystallography. The molecule forms a right-handed helix with a reversal of the sense of the helix at the C-terminus. Torsion angles and hydrogen bonding pattern are consistent with a mixed 3(10)-/alpha-helical conformation. In the crystal, continuous columns are formed by head-to-tail arrangement of hydrogen-bonded molecules along the helix axis. The helical columns associate via hydrogen bonds forming closely packed parallel pairs.
authors.affiliation: IMBB/FORTH Crete, Greece.
authors.forename: R
authors.initials: R
authors.lastname: Gessmann
authors.forename: H
authors.initials: H
authors.lastname: Brueckner
authors.forename: M
authors.initials: M
authors.lastname: Kokkinidis
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D009842:Oligopeptides; D010446:Peptide Fragments; D010455:Peptides; C076329:benzyloxycarbonyl-alpha-aminoisobutyryl-glycyl-alpha-aminoisobutyryl-leucyl-alpha-aminoisobutyryl-tert-butyl ester; C016161:trichotoxin