Solution structure and backbone dynamics of the biotinylation domain of Helicobacter pylori biotin-carboxyl carrier protein

Jinwon Jung, Chul Jin Lee, Young Ho Jeon, Chaejoon Cheong, Weontae Lee

Research output: Contribution to journalArticle


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 β-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.

Original languageEnglish
Pages (from-to)347-351
Number of pages5
JournalBulletin of the Korean Chemical Society
Issue number2
Publication statusPublished - 2008 Feb 20


All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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