Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Solution Structure and Backbone Dynamics of the Biotinylation Domain of Helicobacter pylori Biotin-carboxyl Carrier Protein

  • Jung, Jin-Won (Department of Biochemistry and Protein Network Research Center, College of Science, Yonsei University) ;
  • Lee, Chul-Jin (Department of Biochemistry and Protein Network Research Center, College of Science, Yonsei University) ;
  • Jeon, Young-Ho (Magnetic Resonance Team, Korea Basic Science Institute (KBSI)) ;
  • Cheong, Chae-Joon (Magnetic Resonance Team, Korea Basic Science Institute (KBSI)) ;
  • Lee, Weon-Tae (Department of Biochemistry and Protein Network Research Center, College of Science, Yonsei University)
  • Published : 2008.02.20
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Abstract

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.

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