Magnetic Resonance
Magnetic Resonance
MR
Articles | Volume 3, issue 1
Articles | Volume 3, issue 1
https://doi.org/10.5194/mr-3-1-2022
© Author(s) 2022. This work is distributed under
the Creative Commons Attribution 4.0 License.
https://doi.org/10.5194/mr-3-1-2022
© Author(s) 2022. This work is distributed under
the Creative Commons Attribution 4.0 License.
Articles | Volume 3, issue 1
Research article
 | 
04 Jan 2022
Research article |  | 04 Jan 2022

Localising individual atoms of tryptophan side chains in the metallo-β-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites

Henry W. Orton, Iresha D. Herath, Ansis Maleckis, Shereen Jabar, Monika Szabo, Bim Graham, Colum Breen, Lydia Topping, Stephen J. Butler, and Gottfried Otting

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Latest update: 25 Dec 2024
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Short summary
This paper explores a method for determining the solution structure of a solvent-exposed polypeptide segment (the L3 loop), which is next to the active site of the penicillin-degrading enzyme IMP-1. Tagging three different sites on the protein with paramagnetic metal ions allowed positioning of the L3 loop with atomic resolution. It was found that the method was more robust when omitting data obtained with different metal ions if obtained with the same tag at the same tagging site.
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