Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate

E. Joel Loveridge, Stella M. Matthews, Christopher Williams, Sara B.M. Whittaker, Ulrich L. Günther, Rhiannon M. Evans, William M. Dawson, Matthew P. Crump, Rudolf K. Allemann*

*Corresponding author for this work
2 Citations (Scopus)

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.

Original languageEnglish
JournalBiomolecular NMR Assignments
Volume7
Issue number1
Pages (from-to)61-64
Number of pages4
ISSN1874-2718
DOIs
Publication statusPublished - 04.2013

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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