Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate
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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.
KeywordsDihydrofolate reductase Moritella profunda Conformational heterogeneity
DHFR from Escherichia coli
DHFR from Moritella profunda
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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