Articles | Volume 3, issue 2
Research article
13 Sep 2022
Research article |  | 13 Sep 2022

Site-selective generation of lanthanoid binding sites on proteins using 4-fluoro-2,6-dicyanopyridine

Sreelakshmi Mekkattu Tharayil, Mithun C. Mahawaththa, Akiva Feintuch, Ansis Maleckis, Sven Ullrich, Richard Morewood, Michael J. Maxwell, Thomas Huber, Christoph Nitsche, Daniella Goldfarb, and Gottfried Otting

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Cited articles

Abdelkader, E. H., Feintuch, A., Yao, X., Adams, L. A., Aurelio, L., Graham, B., Goldfarb, D., and Otting, G.: Protein conformation by EPR spectroscopy using gadolinium tags clicked to genetically encoded p-azido-l-phenylalanine, Chem. Commun., 51, 15898–15901,, 2015. 
Bahrenberg, T., Rosenski, Y., Carmieli, R., Zibzener, K., Qi, M., Frydman, V., Godt, A., Goldfarb, D., and Feintuch, A.: Improved sensitivity for W-band Gd(III)-Gd(III) and nitroxide-nitroxide DEER measurements with shaped pulses, J. Magn. Reson., 283, 1–13,, 2017. 
Barak, N. N., Neumann, P., Sevvana, M., Schutkowski, M., Naumann, K., Malešević, M., Reichardt, H., Fischer, G., Stubbs, M. T., and Ferrari, D. M.: Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29, J. Mol. Biol., 385, 1630–1642,, 2009. 
Bertini, I., Luchinat, C., and Parigi, G.: Magnetic susceptibility in paramagnetic NMR, Prog. Nucl. Mag. Res. Sp., 40, 211–236,, 2002. 
Collauto, A., Frydman, V., Lee, M., Abdelkader, E., Feintuch, A., Swarbrick, J., Graham, B., Otting, G., and Goldfarb, D.: RIDME distance measurements using Gd(III) tags with a narrow central transition, Phys. Chem. Chem. Phys., 18, 19037–19049,, 2016. 
Short summary
Having shown that tagging a protein at a single site with different lanthanoid complexes delivers outstanding structural information at a selected site of a protein (such as active sites and ligand binding sites), we now present a simple way by which different lanthanoid complexes can be assembled on a highly solvent-exposed cysteine residue. Furthermore, the chemical assembly is selective for selenocysteine, if a selenocysteine residue can be introduced into the protein of interest.