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

Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been super(13)C/ super(15)N isotopically labelled and purified. Here, we report the aliphatic super(1)H, super(13)C and super(15)N resonance assignments of MpDHFR in complex with NADP super(+) and folate. The spectra...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2013-04, Vol.7 (1), p.61-64
Main Authors: Loveridge, EJoel, Matthews, Stella M, Williams, Christopher, Whittaker, Sara B-M, Guenther, Ulrich L, Evans, Rhiannon M, Dawson, William M, Crump, Matthew P, Allemann, Rudolf K
Format: Article
Language:English
Subjects:
Dihydrofolate reductase
Escherichia coli
Folic acid
Moritella
N.M.R
Online Access:Get full text
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Summary:Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been super(13)C/ super(15)N isotopically labelled and purified. Here, we report the aliphatic super(1)H, super(13)C and super(15)N resonance assignments of MpDHFR in complex with NADP super(+) and folate. The spectra of MpDHFR suggest considerably greater conformational heterogeneity than is seen in the closely related DHFR from Escherichia coli.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-012-9378-x