Abstract
Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been 13C/15N isotopically labelled and purified. Here, we report the aliphatic 1H, 13C and 15N resonance assignments of MpDHFR in complex with NADP+ and folate. The spectra of MpDHFR suggest considerably greater conformational heterogeneity than is seen in the closely related DHFR from Escherichia coli.
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Abbreviations
- DHFR:
-
Dihydrofolate reductase
- EcDHFR:
-
DHFR from Escherichia coli
- MpDHFR:
-
DHFR from Moritella profunda
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Acknowledgments
This work was supported by the UK’s Biotechnology and Biological Sciences Research Council (BBSRC) through grant BB/E008380/1 and Cardiff University. We thank the Wellcome Trust for open access to the Varian INOVA 900 MHz spectrometer at HWB-NMR, University of Birmingham, through Biomedical Resources grant 083796/Z/07/Z. We also thank the Wellcome Trust (WT082352MA) and the Engineering and Physical Sciences Research Council (EPSRC) (EP/F013515) for the Varian VNMRS 600 MHz cryo-probe at the University of Bristol.
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Loveridge, E.J., Matthews, S.M., Williams, C. et al. Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate. Biomol NMR Assign 7, 61–64 (2013). https://doi.org/10.1007/s12104-012-9378-x
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DOI: https://doi.org/10.1007/s12104-012-9378-x