Domain Z7 of nuclear transcription factor ZNF711 has the consensus last metal-ligand H23 found in odd-numbered zinc fingers of this protein replaced by a phenylalanine. Ever since the discovery of ZNF711, it has been thought that Z7 is probably non-functional because of the H23F substitution. The presence of H26 three positions downstream prompted us to examine if this histidine could substitute as the last metal-ligand. The Z7 domain adopts a stable tertiary structure upon metal-binding. The...
[NMR paper] Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure
Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure
Domain Z7 of nuclear transcription factor ZNF711 has the consensus last metal-ligand H23 found in odd-numbered zinc-fingers of this protein replaced by a phenylalanine. Ever since the discovery of ZNF711 it has been thought that Z7 is probably non-functional because of the H23F substitution. The presence of H26 three positions downstream prompted us to examine if this histidine could substitute as the last metal ligand. The Z7 domain adopts a stable tertiary structure...
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04-24-2024 05:58 AM
[NMR paper] Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure
Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure
It is increasingly recognized that very small proteins (?-proteins) are ubiquitously found in all species of the three domains of life, and that they fulfill important functions. The halophilic archaeon Haloferax volcanii contains 282 ?-proteins of less than 70 amino acids. Notably, 43 of these contain two C(P)XCG motifs, suggesting their potential to complex a zinc ion. To explore the significance of these proteins, 16 genes encoding C(P)XCG proteins...
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12-15-2023 05:49 AM
[NMR paper] NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750
NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750
ZNF750 is a nuclear transcription factor that activates skin differentiation and has tumor suppressor roles in several cancers. Unusually, ZNF750 has only a single zinc-finger (ZNF) domain, Z*, with an amino acid sequence that differs markedly from the CCHH family consensus. Because of its sequence differences Z* is classified as degenerate, presumed to have lost the ability to bind the zinc ion required for folding. AlphaFold predicts an irregular structure for Z* with low confidence. Low...
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09-02-2023 01:54 AM
[NMR paper] NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750
NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750
ZNF750 is a nuclear transcription factor that activates skin differentiation and has tumor suppressor roles in several cancers. Unusually, ZNF750 has only a single zinc-finger (ZNF) domain, Z*, with an amino acid sequence that differs markedly from the CCHH family consensus. Because of its sequence differences Z* is classified as degenerate, presumed to have lost the ability to bind the zinc ion required for folding. AlphaFold predicts an irregular structure for Z* with low confidence. Low...
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07-25-2023 01:43 PM
[NMR paper] Zinc finger structure determination by NMR: Why zinc fingers can be a handful
Zinc finger structure determination by NMR: Why zinc fingers can be a handful
Zinc fingers can be loosely defined as protein domains containing one or more tetrahedrally-co-ordinated zinc ions whose role is to stabilise the structure rather than to be involved in enzymatic chemistry; such zinc ions are often referred to as "structural zincs". Although structural zincs can occur in proteins of any size, they assume particular significance for very small protein domains, where they are often essential for maintaining a folded state. Such small structures, that sometimes...
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[ASAP] Overcharging of the Zinc Ion in the Structure of the Zinc-Finger Protein Is Needed for DNA Binding Stability
Overcharging of the Zinc Ion in the Structure of the Zinc-Finger Protein Is Needed for DNA Binding Stability
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01055/20200220/images/medium/bi9b01055_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01055
http://feeds.feedburner.com/~r/acs/bichaw/~4/un5QBZFhB-o
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02-29-2020 09:52 PM
[NMR paper] NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana S
NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein.
Related Articles NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein.
Chembiochem. 2003 Mar 3;4(2-3):171-80
Authors: Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R
Zinc finger domains of the classical type represent the most abundant DNA binding domains in eukaryotic transcription factors. Plant proteins...
Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure
Linear Mode
