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Progress in Chemistry 2019, Vol. 31 Issue (10): 1372-1383 DOI: 10.7536/PC190310 Previous Articles   Next Articles

Structures, Properties, and Applications of Metalloregulatory Proteins

Yanan Zheng, Dan Wang**()   

  1. College of Chemistry and Materials, Nanning Normal University, Nanning 530001, China
  • Received: Online: Published:
  • Contact: Dan Wang
  • About author:
    ** E-mail:
  • Supported by:
    National Natural Science Foundation of China(31800631); Natural Science Foundation of Guangxi Province(2018JJB120049); Middle-aged and Young Teachers’ Basic Ability Promotion Project of Guangxi(2018KY0361)
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The metalloregulatory protein is the metal-specific binding protein in microorganisms that tightly regulates the intake, efflux, and storage of the metal ions through the regulatory mechanism of transcriptional repression or activation, which is particularly important for the maintaining of suitable metal concentration and homeostasis. In this review, the regulatory mechanism and topological structure are summarized within the current seven major families of metalloregulatory proteins, and the structural feature and metal-ligand coordination geometry of metal-binding domain are also introduced in detail. Based on the metal-ligand coordination geometry, the mechanisms are discussed for the metal selectivity of metalloregulatory proteins. In addition, the applications of metalloregulatory proteins in metal-ion detection and adsorption are also introduced, which not only broadens the research and application areas of metalloregulatory proteins, but also exploits new direction for the bioinorganic chemistry research.

Key words: metalloregulatory protein, metal ions, regulatory mechanism, topological structure, coordination geometry
Fig. 1 Ribbon diagrams of crystallographic structures of B. subtilis PerR. The oxidized form of PerR, designated PerR-Zn-ox, is shown in the top. The Mn(Ⅱ)-activated PerR, designated PerR-Zn-Mn, is shown in the bottom
Fig. 2 Ribbon diagrams of crystallographic structures and metal-binding sites of B. subtilis MntR. The N-terminal DNA-binding domain of apo-MntR(PDB: 2HYF) is shown as green, and the N-terminal DNA-binding domain of metal-bound MntR(PDB: 2F5F) is shown as blue
Fig. 3 Ribbon diagrams of crystallographic structures of E. coli DNA-Ni(Ⅱ)-NikR complex
Fig. 4 Ribbon diagrams of crystallographic structures of E. coli CueR. The metal-free CueR is shown on the left, and the metal-bound CueR is shown on the right
Fig. 5 Summary of the known metal binding sites of ArsR/SmtB family repressors on the structure of S. aureus pI258 CadC homodimer. The Zn(Ⅱ)-binding site α5 and Cd(Ⅱ)-binding site in pI258 CadC homodimer α3 N are shown in the right, which correspond to the red and yellow part in the left. Other metal-binding sites in the ArsR/SmtB family repressors are shown in the left
Fig. 6 Summary of the known metal binding sites and feature sequence domain of CosR/RcnR family repressors on the structure of M. tuberculosis CosR. The M. tuberculosis CosR coordinate Cu(Ⅰ) through the residues Cys36, His61’ and Cys65’. The E. coli RcnR coordinate Ni(Ⅱ) through the residues in the feature sequence domain W-X-Y-Z
Fig. 7 (a) The designed fluorescence probe based on the allosteric transcriptional regulation mechanism of MerR family members MerR, CueR, and PbrR.(b) The protein engineering based on the metalloregulatory protein NikR [77~79, 83]
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