ArticleBiochemistry2008
Structural basis of the metal specificity for nickel regulatory protein NikR.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 55 citations in OpenAlex.
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Mechanistic insights into the nickel-dependent allosteric response of the Helicobacter pylori NikR transcription factor.The Journal of biological chemistry · 2023Article
- A study on the secondary structure of the metalloregulatory protein CueR: effect of pH, metal ions and DNA.European biophysics journal : EBJ · 2021Article
- C-terminal Cysteines of CueR Act as Auxiliary Metal Site Ligands upon HgChemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- The Electronic Structure of the Metal Active Site Determines the Geometric Structure and Function of the Metalloregulator NikR.Biochemistry · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- The Irving-Williams series and the 2-His-1-carboxylate facial triad: a thermodynamic study of MnJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Metal specificity of cyanobacterial nickel-responsive repressor InrS: cells maintain zinc and copper below the detection threshold for InrS.Molecular microbiology · 2014Article
- Ni(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Metalloregulatory proteins: metal selectivity and allosteric switching.Biophysical chemistry · 2011Review
- Holo-Ni(II)HpNikR is an asymmetric tetramer containing two different nickel-binding sites.Journal of the American Chemical Society · 2010Article
- Searching for the Nik operon: how a ligand-responsive transcription factor hunts for its DNA binding site.Biochemistry · 2010Article
- Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli.Biochemistry · 2010Article
- Structural and mechanistic insights into Helicobacter pylori NikR activation.Nucleic acids research · 2010Article
- A turn-on fluorescent sensor for detecting nickel in living cells.Journal of the American Chemical Society · 2009Article
- Apo and nickel-bound forms of the Pyrococcus horikoshii species of the metalloregulatory protein: NikR characterized by molecular dynamics simulations.Biochemistry · 2009Article
- Coordination chemistry of bacterial metal transport and sensing.Chemical reviews · 2009Review
- Metalloproteins and metal sensing.Nature · 2009Review
- Physical basis of metal-binding specificity in Escherichia coli NikR.Journal of the American Chemical Society · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
In the presence of excess nickel, Escherichia coli NikR regulates cellular nickel uptake by suppressing the transcription of the nik operon, which encodes the nickel uptake transporter, NikABCDE. Previously published in vitro studies have shown that NikR is capable of binding a range of divalent transition metal ions in addition to Ni2+, including Co2+, Cu2+, Zn2+, and Cd2+. To understand how the high-affinity nickel binding site of NikR is able to accommodate these other metal ions, and to improve our understanding of NikR's mechanism of binding to DNA, we have determined structures of the metal-binding domain (MBD) of NikR in the apo form and in complex with Cu2+ and Zn2+ ions and compared them with the previously published structures with Ni2+. We observe that Cu2+ ions bind in a manner very similar to that of Ni2+, with a square planar geometry but with longer bond lengths. Crystals grown in the presence of Zn2+ reveal a protein structure similar to that of apo MBD with a disordered alpha3 helix, but with two electron density peaks near the Ni2+ binding site corresponding to two Zn2+ ions. These structural findings along with biochemical data on NikR support a hypothesis that ordering of the alpha3 helix is important for repressor activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.