An unusual reverse turn structure adopted by a furanoid sugar amino acid incorporated in gramicidin S

Gijsbert M Grotenbreg; Mattie S M Timmer; Antonio L Llamas-Saiz; Martijn Verdoes; Gijsbert A van der Marel; Mark J van Raaij; Herman S Overkleeft; Mark Overhand

doi:10.1021/ja0397254

An unusual reverse turn structure adopted by a furanoid sugar amino acid incorporated in gramicidin S

J Am Chem Soc. 2004 Mar 24;126(11):3444-6. doi: 10.1021/ja0397254.

Authors

Gijsbert M Grotenbreg¹, Mattie S M Timmer, Antonio L Llamas-Saiz, Martijn Verdoes, Gijsbert A van der Marel, Mark J van Raaij, Herman S Overkleeft, Mark Overhand

Affiliation

¹ Leiden Institute of Chemistry, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.

PMID: 15025470
DOI: 10.1021/ja0397254

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acids / chemistry*
Amino Sugars / chemistry*
Furans / chemistry*
Gramicidin / chemical synthesis
Gramicidin / chemistry*
Models, Molecular
Protein Conformation

Substances

Amino Acids
Amino Sugars
Furans
Gramicidin