Abstract
Cyclophilins regulate protein folding, transport and signalling through catalysis of proline isomerization, and are ubiquitously expressed in both prokaryotes and eukaryotes. Cpr3 is the yeast mitochondrial cyclophilin and it is structurally and biophysically uncharacterized so far. Yeast cyclophilin gene cpr3 is essential for the lactate metabolism. Here, we report 1H, 13C, and 15N chemical shift assignments of Cpr3 protein determined by various 2D and 3D heteronuclear NMR experiments at pH 6.5, and temperature 298 K.
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Acknowledgments
We are thankful to RIFC, IRCC, NMR facility (750 MHz) at IIT Bombay.V.K.S is the recipients of research fellowships from DAE, Mumbai, India. J.S.S and D.T. are recipients of research fellowships from MHRD, IIT Bombay, Mumbai, India.
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Shukla, V.K., Singh, J.S., Trivedi, D. et al. NMR assignments of mitochondrial cyclophilin Cpr3 from Saccharomyces cerevisiae . Biomol NMR Assign 10, 203–206 (2016). https://doi.org/10.1007/s12104-016-9667-x
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DOI: https://doi.org/10.1007/s12104-016-9667-x