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

doi:10.1007/s12104-012-9378-x

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^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Chemie und Metabolomics

2 Zitate (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.

Originalsprache	Englisch
Zeitschrift	Biomolecular NMR Assignments
Jahrgang	7
Ausgabenummer	1
Seiten (von - bis)	61-64
Seitenumfang	4
ISSN	1874-2718
DOIs	https://doi.org/10.1007/s12104-012-9378-x
Publikationsstatus	Veröffentlicht - 04.2013

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10.1007/s12104-012-9378-x

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Loveridge, E. J., Matthews, S. M., Williams, C., Whittaker, S. B. M., Günther, U. L., Evans, R. M., Dawson, W. M., Crump, M. P., & Allemann, R. K. (2013). Aliphatic ¹H, ¹³C and ¹⁵N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP⁺ and folate. Biomolecular NMR Assignments, 7(1), 61-64. https://doi.org/10.1007/s12104-012-9378-x

@article{dbd28e7bc1aa45e2b279064c8d1d3080,

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

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.",

author = "Loveridge, {E. Joel} and Matthews, {Stella M.} and Christopher Williams and Whittaker, {Sara B.M.} and G{\"u}nther, {Ulrich L.} and Evans, {Rhiannon M.} and Dawson, {William M.} and Crump, {Matthew P.} and Allemann, {Rudolf K.}",

note = "Funding Information: Acknowledgments This work was supported by the UK{\textquoteright}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. Copyright: Copyright 2013 Elsevier B.V., All rights reserved.",

year = "2013",

month = apr,

doi = "10.1007/s12104-012-9378-x",

language = "English",

volume = "7",

pages = "61--64",

journal = "Biomolecular NMR Assignments",

issn = "1874-2718",

number = "1",

}

Loveridge, EJ, Matthews, SM, Williams, C, Whittaker, SBM, Günther, UL, Evans, RM, Dawson, WM, Crump, MP & Allemann, RK 2013, 'Aliphatic ¹H, ¹³C and ¹⁵N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP⁺ and folate', Biomolecular NMR Assignments, Jg. 7, Nr. 1, S. 61-64. https://doi.org/10.1007/s12104-012-9378-x

Aliphatic ¹H, ¹³C and ¹⁵N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP⁺ and folate. / Loveridge, E. Joel; Matthews, Stella M.; Williams, Christopher et al.
in: Biomolecular NMR Assignments, Jahrgang 7, Nr. 1, 04.2013, S. 61-64.

Publikation: Beiträge in Fachzeitschriften › Zeitschriftenaufsätze › Forschung › Begutachtung

TY - JOUR

T1 - Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate

AU - Loveridge, E. Joel

AU - Matthews, Stella M.

AU - Williams, Christopher

AU - Whittaker, Sara B.M.

AU - Günther, Ulrich L.

AU - Evans, Rhiannon M.

AU - Dawson, William M.

AU - Crump, Matthew P.

AU - Allemann, Rudolf K.

N1 - Funding Information: Acknowledgments 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. Copyright: Copyright 2013 Elsevier B.V., All rights reserved.

PY - 2013/4

Y1 - 2013/4

N2 - 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.

AB - 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.

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U2 - 10.1007/s12104-012-9378-x

DO - 10.1007/s12104-012-9378-x

M3 - Journal articles

C2 - 22415546

AN - SCOPUS:84874997943

SN - 1874-2718

VL - 7

SP - 61

EP - 64

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

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ER -