An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S

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‘ β-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 an...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of the American Chemical Society 2004-03, Vol.126 (11), p.3444-3446
Hauptverfasser: Grotenbreg, Gijsbert M, Timmer, Mattie S. M, Llamas-Saiz, Antonio L, Verdoes, Martijn, van der Marel, Gijsbert A, van Raaij, Mark J, Overkleeft, Herman S, Overhand, Mark
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acids - chemistry
Amino Sugars - chemistry
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Furans - chemistry
Gramicidin - chemical synthesis
Gramicidin - chemistry
Models, Molecular
Protein Conformation
Proteins
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:A new reverse turn, replacing one of the native type II‘ β-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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0397254