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Related Experiment Videos

Structural elements of metal selectivity in metal sensor proteins.

Mario A Pennella1, Jacob E Shokes, Nathaniel J Cosper

  • 1Department of Biochemistry and Biophysics, Center for Advanced Biomolecular Research, Texas A&M University, College Station, TX 77843-2128, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 26, 2003
PubMed
Summary

Staphylococcus aureus CzrA and Mycobacterium tuberculosis NmtR are bacterial metal-sensing proteins. Their metal regulation differs, with CzrA responding most strongly to zinc, and NmtR to nickel.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Staphylococcus aureus CzrA and Mycobacterium tuberculosis NmtR are homologous prokaryotic metal sensor proteins.
  • They function as transcriptional repressors, responding to different metal ions in vivo.

Purpose of the Study:

  • To investigate the in vitro metal ion regulation of CzrA and NmtR DNA binding.
  • To characterize the metal coordination complexes of CzrA and NmtR.
  • To understand the structural basis for differential metal sensing.

Main Methods:

  • In vitro operator-promoter binding assays.
  • UV-visible spectroscopy.
  • X-ray absorption spectroscopy.
  • Sequence analysis.

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Main Results:

  • Zn(II) is the most potent regulator for CzrA (Zn(II)>Co(II)>Ni(II)), while Ni(II) is most potent for NmtR (Ni(II)>Co(II)>Zn(II)).
  • CzrA forms four-coordinate metal complexes (Zn(II), Co(II)) that potently regulate DNA binding.
  • NmtR forms five- or six-coordinate complexes (Ni(II), Co(II)) that are strong allosteric regulators, uniquely recruiting additional ligands.

Conclusions:

  • Differential metal ion sensing by CzrA and NmtR is determined by their distinct metal coordination environments.
  • The conserved His-3-carboxylate motif is crucial for Zn(II) binding in both proteins.
  • NmtR's flexible C-terminal region allows for expanded coordination and differential metal response.