ArticleScientific reports2016
Classification of the treble clef zinc finger: noteworthy lessons for structure and function evolution.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 22 citations in OpenAlex.
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- Identification of genetic markers of resistance to macrolide class antibiotics inApplied and environmental microbiology · 2024Article
- The unusual structure of the PiggyMac cysteine-rich domain reveals zinc finger diversity in PiggyBac-related transposases.Mobile DNA · 2021Article
- Harnessing the potential of plant transcription factors in developing climate resilient crops to improve global food security: Current and future perspectives.Saudi journal of biological sciences · 2021Review
- Beyond Arabidopsis: BBX Regulators in Crop Plants.International journal of molecular sciences · 2021Review
- The Novel Halovirus Hardycor1, and the Presence of Active (Induced) Proviruses in Four Haloarchaea.Genes · 2021Article
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- Evolutionary convergence and divergence in archaeal chromosomal proteins and Chromo-like domains from bacteria and eukaryotes.Scientific reports · 2018Article
- Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB.Structure (London, England : 1993) · 2018Article
- Review
- Systematic classification of the His-Me finger superfamily.Nucleic acids research · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Treble clef (TC) zinc fingers constitute a large fold-group of structural zinc-binding protein domains that mediate numerous cellular functions. We have analysed the sequence, structure, and function relationships among all TCs in the Protein Data Bank. This led to the identification of novel TCs, such as lsr2, YggX and TFIIIC τ 60 kDa subunit, and prediction of a nuclease-like function for the DUF1364 family. The structural malleability of TCs is evident from the many examples with variations to the core structural elements of the fold. We observe domains wherein the structural core of the TC fold is circularly permuted, and also some examples where the overall fold resembles both the TC motif and another unrelated fold. All extant TC families do not share a monophyletic origin, as several TC proteins are known to have been present in the last universal common ancestor and the last eukaryotic common ancestor. We identify several TCs where the zinc-chelating site and residues are not merely responsible for structure stabilization but also perform other functions, such as being redox active in C1B domain of protein kinase C, a nucleophilic acceptor in Ada and catalytic in organomercurial lyase, MerB.
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