3-mercapto-2, 6-pyridinedicarboxylic acid: A small lanthanide-binding tag for protein studies by NMR spectroscopy

Bradley Man; Xun Cheng Su; Haobo Liang; Shane Simonsen; Thomas Huber; Barbara A. Messerle; Gottfried Otting

doi:10.1002/chem.200902904

3-mercapto-2, 6-pyridinedicarboxylic acid: A small lanthanide-binding tag for protein studies by NMR spectroscopy

Bradley Man, Xun Cheng Su, Haobo Liang, Shane Simonsen, Thomas Huber, Barbara A. Messerle, Gottfried Otting^*

^*Corresponding author for this work

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

47 Citations (Scopus)

Abstract

Paramagnetic effects from lanthanide ions present powerful tools for protein studies by nuclear magnetic resonance (NMR) spectroscopy provid-ed that the lanthanide can be site-spe-cifically and rigidly attached to the pro-tein. A new, particularly small and rigid lanthanide-binding tag, 3-mercap-to-2, 6-pyridinedicarboxylic acid (3MDPA), was synthesized and at-tached to two different proteins via a disulfide bond. The complexes of the N-terminal domain of the E. coli argi-nine repressor (ArgN) with seven dif-ferent paramagnetic lanthanide ions and Co²⁺ were analyzed in detail by NMR spectroscopy. The magnetic sus-ceptibility anisotropy (ΔX) tensors and metal position were determined from pseudocontact shifts. The 3MDPA tag generated very different Ax tensor ori-entations compared to the previously studied 4-mercaptomethyl-DPA tag, making it a highly complementary and useful tool for protein NMR studies.

Original language	English
Pages (from-to)	3827-3832
Number of pages	6
Journal	Chemistry - A European Journal
Volume	16
Issue number	12
DOIs	https://doi.org/10.1002/chem.200902904
Publication status	Published - 22 Mar 2010

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title = "3-mercapto-2, 6-pyridinedicarboxylic acid: A small lanthanide-binding tag for protein studies by NMR spectroscopy",

abstract = "Paramagnetic effects from lanthanide ions present powerful tools for protein studies by nuclear magnetic resonance (NMR) spectroscopy provid-ed that the lanthanide can be site-spe-cifically and rigidly attached to the pro-tein. A new, particularly small and rigid lanthanide-binding tag, 3-mercap-to-2, 6-pyridinedicarboxylic acid (3MDPA), was synthesized and at-tached to two different proteins via a disulfide bond. The complexes of the N-terminal domain of the E. coli argi-nine repressor (ArgN) with seven dif-ferent paramagnetic lanthanide ions and Co2+ were analyzed in detail by NMR spectroscopy. The magnetic sus-ceptibility anisotropy (ΔX) tensors and metal position were determined from pseudocontact shifts. The 3MDPA tag generated very different Ax tensor ori-entations compared to the previously studied 4-mercaptomethyl-DPA tag, making it a highly complementary and useful tool for protein NMR studies.",

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AU - Simonsen, Shane

AU - Huber, Thomas

AU - Messerle, Barbara A.

AU - Otting, Gottfried

PY - 2010/3/22

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KW - Lanthanides

KW - Magnetic properties

KW - NMR spec-troscopy

KW - Protein labeling

KW - Pseudocontact shifts

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3-mercapto-2, 6-pyridinedicarboxylic acid: A small lanthanide-binding tag for protein studies by NMR spectroscopy

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