Two Histidines in an α-Helix: A Rigid Co2+-Binding Motif for PCS Measurements by NMR Spectroscopy

Alireza Bahramzadeh, Hailun Jiang, Thomas Huber, Gottfried Otting*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    9 Citations (Scopus)

    Abstract

    Pseudocontact shifts (PCS) generated by paramagnetic metal ions present valuable long-range information in the study of protein structural biology by nuclear magnetic resonance (NMR) spectroscopy. Faithful interpretation of PCSs, however, requires complete immobilization of the metal ion relative to the protein, which is difficult to achieve with synthetic metal tags. We show that two histidine residues in sequential turns of an α-helix provide a binding site for a Co2+ ion, which positions the metal ion in a uniquely well-defined and predictable location. Exchange between the bound and free cobalt is slow on the timescale defined by chemical shifts, but the NMR resonance assignments are nonetheless readily transferred from the diamagnetic to the paramagnetic NMR spectrum by an IzSz-exchange experiment. The double-histidine-Co2+ motif offers a straightforward, inexpensive, and convenient way of generating precision PCSs in proteins.

    Original languageEnglish
    Pages (from-to)6226-6229
    Number of pages4
    JournalAngewandte Chemie - International Edition
    Volume57
    Issue number21
    DOIs
    Publication statusPublished - 22 May 2018

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