|Journal of Biochemistry and Molecular Biology (2005) 38(5):550-4|
|Northeast Structural Genomics Consortium|
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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 beta2 and beta3. 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.
|metabolism chemistry genetics |
|Binding Sites Humans Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Protein Structure, Secondary Oxidation-Reduction Sequence Alignment Protein Folding Nuclear Magnetic Resonance, Biomolecular Saccharomyces cerevisiae Proteins Mitochondrial Proteins Saccharomyces cerevisiae |
|16 (Last update: 03/16/2019 2:26:55pm)|
|J Biochem Mol Biol. 2005 Sep 30;38(5):550-4.|