ArticleJournal of biomolecular NMR2012
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 26 citations in OpenAlex.
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- A flexible loop in the paxillin LIM3 domain mediates its direct binding to integrin β subunits.PLoS biology · 2024Article
- The unusual structure of the PiggyMac cysteine-rich domain reveals zinc finger diversity in PiggyBac-related transposases.Mobile DNA · 2021Article
- Asterix/Gtsf1 links tRNAs and piRNA silencing of retrotransposons.Cell reports · 2021Article
- Sequence-specific DNA binding activity of the cross-brace zinc finger motif of the piggyBac transposase.Nucleic acids research · 2018Article
- Structural and Functional Insights Into Lysostaphin-Substrate Interaction.Frontiers in molecular biosciences · 2018Article
- Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.Scientific reports · 2017Article
- Structural basis for ligand binding to an enzyme by a conformational selection pathway.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'-end processing.RNA (New York, N.Y.) · 2017Article
- pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.Journal of biomolecular NMR · 2014Article
- Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid β-fibrils in a redox cycle.The Journal of biological chemistry · 2014Article
- Article
- Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.Journal of biomolecular NMR · 2013Article
- NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3.Journal of biomolecular NMR · 2013Article
- Synthesis, CP-MAS NMR Characterization, and Antibacterial Activities of Glycine and Histidine Complexes of Cd(SeCN) 2 and Hg(SeCN) 2.Bioinorganic chemistry and applications · 2013Article
- Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold.PloS one · 2013Article
- New insights into histidine triad proteins: solution structure of a Streptococcus pneumoniae PhtD domain and zinc transfer to AdcAII.PloS one · 2013Article
- Zinc finger structure determination by NMR: Why zinc fingers can be a handful.Progress in nuclear magnetic resonance spectroscopyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zinc is the second most abundant metal ion incorporated in proteins, and is in many cases a crucial component of protein three-dimensional structures. Zinc ions are frequently coordinated by cysteine and histidine residues. Whereas cysteines bind to zinc via their unique S(γ) atom, histidines can coordinate zinc with two different coordination modes, either N(δ1) or N(ε2) is coordinating the zinc ion. The determination of this coordination mode is crucial for the accurate structure determination of a histidine-containing zinc-binding site by NMR. NMR chemical shifts contain a vast amount of information on local electronic and structural environments and surprisingly their utilization for the determination of the coordination mode of zinc-ligated histidines has been limited so far to (15)N nuclei. In the present report, we observed that the (13)C chemical shifts of aromatic carbons in zinc-ligated histidines represent a reliable signature of their coordination mode. Using a statistical analysis of (13)C chemical shifts, we show that (13)C(δ2) chemical shift is sensitive to the histidine coordination mode and that the chemical shift difference δ{(13)C(ε1)} - δ{(13)C(δ2)} provides a reference-independent marker of this coordination mode. The present approach allows the direct determination of the coordination mode of zinc-ligated histidines even with non-isotopically enriched protein samples and without any prior structural information.
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