Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-1-2021
https://doi.org/10.5194/mr-2-1-2021
Research article
 | 
06 Jan 2021
Research article |  | 06 Jan 2021

Phosphoserine for the generation of lanthanide-binding sites on proteins for paramagnetic nuclear magnetic resonance spectroscopy

Sreelakshmi Mekkattu Tharayil, Mithun Chamikara Mahawaththa, Choy-Theng Loh, Ibidolapo Adekoya, and Gottfried Otting

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Cited articles

Abdelkader, E. H., Yao, X., Feintuch, A., Adams, L. A., Aurelio, L., Graham, B., Goldfarb, D., and Otting, G.: Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags, J. Biomol. NMR, 64, 39–51, https://doi.org/10.1007/s10858-015-0003-z, 2016. 
Baneyx, F. and Mujacic, M.: Recombinant protein folding and misfolding in Escherichia coli, Nat. Biotechnol., 22, 1399–1408, https://doi.org/10.1038/nbt1029, 2004. 
Barthelmes, D., Gränz, M., Barthelmes, K., Allen, K. N., Imperiali, B., Prisner, T., and Schwalbe, H.: Encoded loop-lanthanide-binding tags for long-range distance measurements in proteins by NMR and EPR spectroscopy, J. Biomol. NMR, 63, 275–282, https://doi.org/10.1007/s10858-015-9984-x, 2015. 
Barthelmes, D., Barthelmes, K., Schnorr, K., Jonker, H. R. A., Bodmer, B., Allen, K. N., Imperiali, B., and Schwalbe, H.: Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β, J. Biomol. NMR, 68, 187–194, https://doi.org/10.1007/s10858-017-0118-5, 2017. 
Barthelmes, K., Reynolds, A. M., Peisach, E., Jonker, H. R. A., DeNunzio, N. J., Allen, K. N., Imperiali, B., and Schwalbe, H.: Engineering encodable lanthanide-binding tags into loop regions of proteins, J. Am. Chem. Soc., 133, 808–819, https://doi.org/10.1021/ja104983t, 2011. 
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Short summary
A new way is presented for creating lanthanide binding sites on proteins using site-specifically introduced phosphoserine residues. The paramagnetic effects of lanthanides generate long-range effects, which contain structural information and are readily measured by NMR spectroscopy. Excellent correlations between experimentally observed and back-calculated pseudocontact shifts attest to very good immobilization of the lanthanide ions relative to the proteins.