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NMR pseudocontact shifts in a symmetric protein homotrimer

Müntener, Thomas and Böhm, Raphael and Atz, Kenneth and Häussinger, Daniel and Hiller, Sebastian. (2020) NMR pseudocontact shifts in a symmetric protein homotrimer. Journal of Biomolecular NMR, 74 (8-9). pp. 413-419.

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Official URL: https://edoc.unibas.ch/79190/

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Abstract

NMR pseudocontact shifts are a valuable tool for structural and functional studies of proteins. Protein multimers mediate key functional roles in biology, but methods for their study by pseudocontact shifts are so far not available. Paramagnetic tags attached to identical subunits in multimeric proteins cause a combined pseudocontact shift that cannot be described by the standard single-point model. Here, we report pseudocontact shifts generated simultaneously by three paramagnetic Tm-M7PyThiazole-DOTA tags to the trimeric molecular chaperone Skp and provide an approach for the analysis of this and related symmetric systems. The pseudocontact shifts were described by a "three-point" model, in which positions and parameters of the three paramagnetic tags were fitted. A good correlation between experimental data and predicted values was found, validating the approach. The study establishes that pseudocontact shifts can readily be applied to multimeric proteins, offering new perspectives for studies of large protein complexes by paramagnetic NMR spectroscopy.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
05 Faculty of Science > Departement Chemie > Chemie > Nuclear Magnetic Resonance (Häussinger)
UniBasel Contributors:Hiller Odermatt, Sebastian and Müntener, Thomas and Böhm, Raphael and Häussinger, Daniel
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Springer
ISSN:0925-2738
e-ISSN:1573-5001
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:11 Mar 2021 11:25
Deposited On:11 Mar 2021 11:25

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