Solution Structure and Backbone Dynamics of the Biotinylation Domain of Helicobacter pylori Biotin-carboxyl Carrier Protein

Acetyl-CoA carboxylase (ACC) is an excellent candidate for antibiotics drug target, which mediates malonyl-CoA synthesis from acetyl-CoA through acetylation process. It is also involved in the committed step of fatty acid synthesis which is essential for living organisms. We have determined the thre...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Bulletin of the Korean Chemical Society 2008, 29(2), , pp.347-351
Hauptverfasser: 정진원, 이철진, 전영호, 이원태, Chaejoon Cheong
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Acetyl-CoA carboxylase (ACC) is an excellent candidate for antibiotics drug target, which mediates malonyl-CoA synthesis from acetyl-CoA through acetylation process. It is also involved in the committed step of fatty acid synthesis which is essential for living organisms. We have determined the three dimensional structure of C terminal domain of HP0371, biotin-carboxyl carrier protein of H. pyroli, in solution state using heteronuclear multi-dimensional NMR spectroscopy. The structure of HP0371 shows a flatten b-sheet fold which is similar with that of E. coli. However, the sequence and structure of protruding thumb are different with that of E. coli and the thumb shows different basis of structural rigidity based on backbone dynamics data. KCI Citation Count: 2
ISSN:0253-2964
1229-5949
DOI:10.5012/bkcs.2008.29.2.347