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Structural basis for metal sensing by CnrX.

Trepreau J, Girard E, Maillard AP, de Rosny E, Petit-Haertlein I, Kahn R, Covès J
J Mol Biol 408 766-79 (2011)
Related entries: 2y39, 2y3b, 2y3g, 2y3h, 3epv

Cited: 19 times
EuropePMC logo PMID: 21414325

Abstract

CnrX is the metal sensor and signal modulator of the three-protein transmembrane signal transduction complex CnrYXH of Cupriavidus metallidurans CH34 that is involved in the setup of cobalt and nickel resistance. We have determined the atomic structure of the soluble domain of CnrX in its Ni-bound, Co-bound, or Zn-bound form. Ni and Co ions elicit a biological response, while the Zn-bound form is inactive. The structures presented here reveal the topology of intraprotomer and interprotomer interactions and the ability of metal-binding sites to fine-tune the packing of CnrX dimer as a function of the bound metal. These data suggest an allosteric mechanism to explain how the complex is switched on and how the signal is modulated by Ni or Co binding. These results provide clues to propose a model for signal propagation through the membrane in the complex.

Articles - 2y3d mentioned but not cited (1)

  1. The X-ray structure of NccX from Cupriavidus metallidurans 31A illustrates potential dangers of detergent solubilization when generating and interpreting crystal structures of membrane proteins. Ziani W, Maillard AP, Petit-Härtlein I, Garnier N, Crouzy S, Girard E, Covès J. J. Biol. Chem. 289 31160-31172 (2014)


Reviews citing this publication (7)

  1. Signaling diversity and evolution of extracytoplasmic function (ECF) σ factors. Mascher T. Curr. Opin. Microbiol. 16 148-155 (2013)
  2. Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function and Distribution. Paget MS. Biomolecules 5 1245-1265 (2015)
  3. The biological occurrence and trafficking of cobalt. Okamoto S, Eltis LD. Metallomics 3 963-970 (2011)
  4. The biological chemistry of the transition metal "transportome" of Cupriavidus metallidurans. Nies DH. Metallomics 8 481-507 (2016)
  5. Nickel-responsive transcriptional regulators. Musiani F, Zambelli B, Bazzani M, Mazzei L, Ciurli S. Metallomics 7 1305-1318 (2015)
  6. Metal-responsive RNA polymerase extracytoplasmic function (ECF) sigma factors. Moraleda-Muñoz A, Marcos-Torres FJ, Pérez J, Muñoz-Dorado J. Mol. Microbiol. 112 385-398 (2019)
  7. The requirement for cobalt in vitamin B12: A paradigm for protein metalation. Osman D, Cooke A, Young TR, Deery E, Robinson NJ, Warren MJ. Biochim Biophys Acta Mol Cell Res 1868 118896 (2021)

Articles citing this publication (11)

  1. The BaeSR regulon is involved in defense against zinc toxicity in E. coli. Wang D, Fierke CA. Metallomics 5 372-383 (2013)
  2. Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae. Lisher JP, Higgins KA, Maroney MJ, Giedroc DP. Biochemistry 52 7689-7701 (2013)
  3. The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors. Maillard AP, Girard E, Ziani W, Petit-Härtlein I, Kahn R, Covès J. J. Mol. Biol. 426 2313-2327 (2014)
  4. Deletion of the zupT gene for a zinc importer influences zinc pools in Cupriavidus metallidurans CH34. Herzberg M, Bauer L, Nies DH. Metallomics 6 421-436 (2014)
  5. Transcriptional regulation by σ factor phosphorylation in bacteria. Iyer SC, Casas-Pastor D, Kraus D, Mann P, Schirner K, Glatter T, Fritz G, Ringgaard S. Nat Microbiol 5 395-406 (2020)
  6. Ratiometric pulse-chase amidination mass spectrometry as a probe of biomolecular complex formation. Chang FM, Lauber MA, Running WE, Reilly JP, Giedroc DP. Anal. Chem. 83 9092-9099 (2011)
  7. Zinc-Induced Transposition of Insertion Sequence Elements Contributes to Increased Adaptability of Cupriavidus metallidurans. Vandecraen J, Monsieurs P, Mergeay M, Leys N, Aertsen A, Van Houdt R. Front Microbiol 7 359 (2016)
  8. Spectroscopic characterization of the metal-binding sites in the periplasmic metal-sensor domain of CnrX from Cupriavidus metallidurans CH34. Trepreau J, de Rosny E, Duboc C, Sarret G, Petit-Hartlein I, Maillard AP, Imberty A, Proux O, Covès J. Biochemistry 50 9036-9045 (2011)
  9. The third pillar of metal homeostasis in Cupriavidus metallidurans CH34: preferences are controlled by extracytoplasmic function sigma factors. Große C, Poehlein A, Blank K, Schwarzenberger C, Schleuder G, Herzberg M, Nies DH. Metallomics 11 291-316 (2019)
  10. Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR. Carr CE, Musiani F, Huang HT, Chivers PT, Ciurli S, Maroney MJ. Inorg Chem 56 6459-6476 (2017)
  11. Coevolutionary Analysis Reveals a Conserved Dual Binding Interface between Extracytoplasmic Function σ Factors and Class I Anti-σ Factors. Casas-Pastor D, Diehl A, Fritz G. mSystems 5 (2020)


Related citations provided by authors (1)

  1. X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms.. Pompidor G, Maillard AP, Girard E, Gambarelli S, Kahn R, Covès J FEBS Lett 582 3954-8 (2008)

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