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

Research output: Contribution to journal › Article › peer-review

Authors

E Joel Loveridge
Stella M Matthews
Sara B-M Whittaker
Rhiannon M Evans
William M Dawson
Matthew P Crump

Colleges, School and Institutes

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.