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.
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.
the Creative Commons Attribution 4.0 License.
Research article
| 
04 Jan 2022
Research article |
| 04 Jan 2022
| 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
ARC Centre of Excellence for Innovations in Peptide & Protein
Science, Research School of Chemistry, Australian National University,
Canberra, ACT 2601, Australia
Iresha D. Herath
Research School of Chemistry, The Australian National University,
Sullivans Creek Road, Canberra ACT 2601, Australia
Ansis Maleckis
Latvian Institute of Organic Synthesis, Aizkraukles 21, 1006 Riga,
Latvia
Shereen Jabar
Research School of Chemistry, The Australian National University,
Sullivans Creek Road, Canberra ACT 2601, Australia
Monika Szabo
Monash Institute of Pharmaceutical Sciences, Monash University,
Parkville, VIC 3052, Australia
Bim Graham
Monash Institute of Pharmaceutical Sciences, Monash University,
Parkville, VIC 3052, Australia
Colum Breen
Department of Chemistry, Loughborough University, Epinal Way, Loughborough, LE11 3TU, United Kingdom
Lydia Topping
Department of Chemistry, Loughborough University, Epinal Way, Loughborough, LE11 3TU, United Kingdom
Stephen J. Butler
Department of Chemistry, Loughborough University, Epinal Way, Loughborough, LE11 3TU, United Kingdom
Gottfried Otting
CORRESPONDING AUTHOR
ARC Centre of Excellence for Innovations in Peptide & Protein
Science, Research School of Chemistry, Australian National University,
Canberra, ACT 2601, Australia
Related authors
Henry W. Orton, Elwy H. Abdelkader, Lydia Topping, Stephen J. Butler, and Gottfried Otting
Magn. Reson., 3, 65–76, https://doi.org/10.5194/mr-3-65-2022, https://doi.org/10.5194/mr-3-65-2022, 2022
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Installing a tag containing a paramagnetic metal ion on a protein can lead to large changes (pseudocontact shifts) in the resonances observed in NMR spectra. These are easily measured and contain valuable long-range structural information. The present work shows that a single tagging site furnished with different tags can be sufficient to localise atoms in proteins with high accuracy. In fact, this strategy works almost as well as the same number of tags distributed over multiple tagging sites.
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The small protein GB1, where all valine residues were replaced by fluorinated analogues containing one or two CH2F groups, produces 19F NMR spectra with exceptional resolution. We establish a convenient strategy for their assignment and analyse the rotameric states of the CH2F groups by virtue of 3-bond coupling constants and a γ-effect on 13C chemical shifts, which is underpinned by DFT calculations. Transient fluorine-fluorine contacts are documented by through-space 19F-19F couplings.
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A protein is produced where a single amino acid type is substituted globally by a fluorinated analogue. Through-space fluorine–fluorine contacts are observed by 19F NMR (nuclear magnetic resonance) spectroscopy. Substitution of methyl groups by CH2F groups yields outstanding spectral resolution with minimal structural perturbation of the protein. Our work identifies the γ-gauche effect as the main reason for the spectral dispersion.
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A novel cell-free protein synthesis system called eCells produces amino acids based on specific isotopes using low-cost precursors. The system selectively labels methyl groups, i.e valine and leucine, with high efficiency. eCells achieve high levels of 13C incorporation and deuteration in protein preparations, making them suitable for NMR experiments of large protein complexes. They are easy to prepare, can be scaled up in volume and are a promising tool for protein production and NMR studies.
Sreelakshmi Mekkattu Tharayil, Mithun C. Mahawaththa, Akiva Feintuch, Ansis Maleckis, Sven Ullrich, Richard Morewood, Michael J. Maxwell, Thomas Huber, Christoph Nitsche, Daniella Goldfarb, and Gottfried Otting
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Having shown that tagging a protein at a single site with different lanthanoid complexes delivers outstanding structural information at a selected site of a protein (such as active sites and ligand binding sites), we now present a simple way by which different lanthanoid complexes can be assembled on a highly solvent-exposed cysteine residue. Furthermore, the chemical assembly is selective for selenocysteine, if a selenocysteine residue can be introduced into the protein of interest.
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Magn. Reson., 3, 65–76, https://doi.org/10.5194/mr-3-65-2022, https://doi.org/10.5194/mr-3-65-2022, 2022
Short summary
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Installing a tag containing a paramagnetic metal ion on a protein can lead to large changes (pseudocontact shifts) in the resonances observed in NMR spectra. These are easily measured and contain valuable long-range structural information. The present work shows that a single tagging site furnished with different tags can be sufficient to localise atoms in proteins with high accuracy. In fact, this strategy works almost as well as the same number of tags distributed over multiple tagging sites.
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A new way is presented for creating lanthanide binding sites on proteins using site-specifically introduced phosphoserine residues. The paramagnetic effects of lanthanides generate long-range effects, which contain structural information and are readily measured by NMR spectroscopy. Excellent correlations between experimentally observed and back-calculated pseudocontact shifts attest to very good immobilization of the lanthanide ions relative to the proteins.
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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.
This paper explores a method for determining the solution structure of a solvent-exposed...
