Two histidines in an alpha-helix: rigid Co2+-binding motif for PCS measurements by NMR spectroscopy.
Angew Chem Int Ed Engl. 2018 Apr 06;:
Authors: Bahramzadeh A, Jiang H, Huber T, Otting G
Abstract
Pseudocontact shifts (PCS) generated by paramagnetic metal ions present valuable long-range information in protein structural biology by nuclear magnetic resonance (NMR) spectroscopy. Faithful interpretation of the PCSs, however, requires complete immobilization of the metal ion relative to the protein, which is difficult to achieve by synthetic metal tags. Here we show that two histidine residues in sequential turns of an alpha-helix provide a binding site for a Co2+ ion, which positions the metal ion in a uniquely well-defined and predictable location. The exchange between 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.
PMID: 29624837 [PubMed - as supplied by publisher]
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Two histidines in an alpha-helix: rigid Co2+-binding motif for PCS measurements by NMR spectroscopy.
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