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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Solution Structure of YKR049C, a Putative Redox Protein from Saccharomyces cerevisiae

  • Jung, Jin-Won (Department of Biochemistry and Protein Network Research Center, Yonsei University) ;
  • Yee, Adelinda (Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto) ;
  • Wu, Bin (Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto) ;
  • Arrowsmith, Cheryl H. (Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto) ;
  • Lee, Weon-Tae (Department of Biochemistry and Protein Network Research Center, Yonsei University)
  • 발행 : 2005.09.30
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초록

YKR049C is a mitochondrial protein in Saccharomyces cerevisiae that is conserved among yeast species, including Candida albicans. However, no biological function for YKR049C has been ascribed based on its primary sequence information. In the present study, NMR spectroscopy was used to determine the putative biological function of YKR049C based on its solution structure. YKR049C shows a well-defined thioredoxin fold with a unique insertion of helices between two $\beta$-strands. The central $\beta$-sheet divides the protein into two parts; a unique face and a conserved face. The 'unique face' is located between ${\beta}2$ and ${\beta}3$. Interestingly, the sequences most conserved among YKR049C families are found on this 'unique face', which incorporates L109 to E114. The side chains of these conserved residues interact with residues on the helical region with a stretch of hydrophobic surface. A putative active site composed by two short helices and a single Cys97 was also well observed. Our findings suggest that YKR049C is a redox protein with a thioredoxin fold containing a single active cysteine.

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