ArticleJournal of the American Chemical Society2009
Energetics of allosteric negative coupling in the zinc sensor S. aureus CzrA.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- A flow equilibrium model controlling cytoplasmic transition metal cation pools and preventing mis-metalation as exemplified for zinc homeostasis.Journal of bacteriology · 2025Review
- A metal-trap tests and refines blueprints to engineer cellular protein metalation with different elements.Nature communications · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Activation of zinc uptake regulator by zinc binding to three regulatory sites.Nucleic acids research · 2024Article
- Characterization of the Zinc Uptake Repressor (Zur) fromBiochemistry · 2024Article
- Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Reveals Buffer-Modulated Cooperativity of Metal-Templated Protein Dimerization.The journal of physical chemistry letters · 2022Article
- Bacterial Transcriptional Regulators: A Road Map for Functional, Structural, and Biophysical Characterization.International journal of molecular sciences · 2022Review
- Allosteric control of metal-responsive transcriptional regulators in bacteria.The Journal of biological chemistry · 2020Review
- Multi-metal Restriction by Calprotectin Impacts De Novo Flavin Biosynthesis in Acinetobacter baumannii.Cell chemical biology · 2019Article
- Functional Role of Solvent Entropy and Conformational Entropy of Metal Binding in a Dynamically Driven Allosteric System.Journal of the American Chemical Society · 2018Article
- Entropy redistribution controls allostery in a metalloregulatory protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Resolution of Stepwise Cooperativities of Copper Binding by the Homotetrameric Copper-Sensitive Operon Repressor (CsoR): Impact on Structure and Stability.Angewandte Chemie (International ed. in English) · 2015Article
- Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.Journal of biomolecular NMR · 2013Article
- Allosteric inhibition of a zinc-sensing transcriptional repressor: insights into the arsenic repressor (ArsR) family.Journal of molecular biology · 2013Article
- Energetics of zinc-mediated interactions in the allosteric pathways of metal sensor proteins.Journal of the American Chemical Society · 2013Article
- Manganese acquisition and homeostasis at the host-pathogen interface.Frontiers in cellular and infection microbiology · 2013Review
- Solution structure of Mycobacterium tuberculosis NmtR in the apo state: insights into Ni(II)-mediated allostery.Biochemistry · 2012Article
- Metal site occupancy and allosteric switching in bacterial metal sensor proteins.Archives of biochemistry and biophysics · 2012Review
- Simulations of allosteric motions in the zinc sensor CzrA.Journal of the American Chemical Society · 2012Article
- Metal ion and DNA binding by single-chain PvuII endonuclease: lessons from the linker.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
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2 authors.
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Abstract
The linked equilibria of an allosterically regulated protein are defined by the structures, residue-specific dynamics and global energetics of interconversion among all relevant allosteric states. Here, we use isothermal titration calorimetry (ITC) to probe the global thermodynamics of allosteric negative regulation of the binding of the paradigm ArsR-family zinc sensing repressor Staphylococcus aureus CzrA to the czr DNA operator (CzrO) by Zn(2+). Zn(2+) binds to the two identical binding sites on the free CzrA homodimer in two discernible steps. A larger entropic driving force Delta(-TDeltaS) of -4.7 kcal mol(-1) and a more negative DeltaC(p) characterize the binding of the first Zn(2+) relative to the second. These features suggest a modest structural transition in forming the Zn(1) state followed by a quenching of the internal dynamics on filling the second zinc site, which collectively drive homotropic negative cooperativity of Zn(2+) binding (Delta(DeltaG) = 1.8 kcal mol(-1)). Negative homotropic cooperativity also characterizes Zn(2+) binding to the CzrA*CzrO complex (Delta(DeltaG) = 1.3 kcal mol(-1)), although the underlying energetics are vastly different, with homotropic Delta(DeltaH) and Delta(-TDeltaS) values both small and slightly positive. In short, Zn(2+) binding to the complex fails to induce a large structural or dynamical change in the CzrA bound to the operator. The strong heterotropic negative linkage in this system (DeltaG(c)(t) = 6.3 kcal mol(-1)) therefore derives from the vastly different structures of the apo-CzrA and CzrA*CzrO reference states (DeltaH(c)(t) = 9.4 kcal mol(-1)) in a way that is reinforced by a global rigidification of the allosterically inhibited Zn(2) state off the DNA (TDeltaS(c)(t) = -3.1 kcal mol(-1), i.e., DeltaS(c)(t) > 0). The implications of these findings for other metalloregulatory proteins are discussed.
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