An unusual reverse turn structure adopted by a furanoid sugar amino acid incorporated in gramicidin S.
A new reverse turn, replacing one of the native type II' beta-turns in the cyclic peptide antibiotic gramicidin S, induced by a furanoid sugar amino acid is revealed. The C3-hydroxyl function plays a pivotal role by acting as a H-bond acceptor, consequently flipping the amide bond between residues i and i + 1, as was established by NMR and X-ray crystallographic analysis.
Grotenbreg
Gijsbert M
GM
Leiden Institute of Chemistry, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Timmer
Mattie S M
MS
Llamas-Saiz
Antonio L
AL
Verdoes
Martijn
M
van der Marel
Gijsbert A
GA
van Raaij
Mark J
MJ
Overkleeft
Herman S
HS
Overhand
Mark
M
D000596:Amino Acids / Q000737:chemistry*; D000606:Amino Sugars / Q000737:chemistry*; D005663:Furans / Q000737:chemistry*; D006096:Gramicidin / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
D000596:Amino Acids; D000606:Amino Sugars; D005663:Furans; D006096:Gramicidin