Aliphatic (1)H, (13)C and (15)N 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

doi:10.1007/s12104-012-9378-x

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

Biomol NMR Assign. 2013 Apr;7(1):61-4. doi: 10.1007/s12104-012-9378-x. Epub 2012 Mar 14.

Authors

E Joel Loveridge¹, Stella M Matthews, Christopher Williams, Sara B-M Whittaker, Ulrich L Günther, Rhiannon M Evans, William M Dawson, Matthew P Crump, Rudolf K Allemann

Affiliation

¹ School of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK.

PMID: 22415546
DOI: 10.1007/s12104-012-9378-x

Abstract

Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been (13)C/(15)N isotopically labelled and purified. Here, we report the aliphatic (1)H, (13)C and (15)N 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Folic Acid / metabolism*
Moritella / enzymology*
NADP / metabolism*
Nuclear Magnetic Resonance, Biomolecular*
Tetrahydrofolate Dehydrogenase / chemistry*
Tetrahydrofolate Dehydrogenase / metabolism*

Substances

NADP
Folic Acid
Tetrahydrofolate Dehydrogenase

Abstract

Publication types

MeSH terms

Substances

Grants and funding