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Cys(x)His(y)-Zn2+ interactions: thiol vs. thiolate coordination.

Thomas Simonson1, Nicolas Calimet

  • 1Department of Structural Biology and Genomics, Institut de Génétique et Biologie Moléculaire et Cellulaire (C.N.R.S.), Strasbourg-Illkirch, France. simonson@igbmc.u-strasbg.fr

Proteins
|September 5, 2002
PubMed
Summary
This summary is machine-generated.

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Thiolate protonation in zinc proteins is possible, especially in Cys4-Zn2+ groups. Theoretical calculations suggest protonation occurs at neutral pH, even in solution, impacting zinc coordination.

Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Structural Biology

Background:

  • Zinc ions (Zn2+) are crucial in proteins, often coordinating tetrahedrally with cysteine and histidine residues.
  • This coordination plays a vital role in protein structure and function, particularly in DNA-binding proteins.

Purpose of the Study:

  • To investigate the potential for thiolate protonation in cysteine-histidine-zinc (Cys(x)His(y)-Zn2+) complexes.
  • To determine the structural and energetic consequences of thiolate protonation in zinc coordination environments.

Main Methods:

  • Analysis of zinc coordination geometries in the Cambridge Structural Database.
  • Ab initio quantum mechanical calculations on model ethanethiolate-imidazole-Zn2+ complexes.
  • Gas phase basicity calculations combined with continuum dielectric solvation models.

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Main Results:

  • Seventy-five percent of surveyed zinc sites exhibit tetrahedral coordination.
  • Protonation of thiolates significantly increases Zn-S bond distances, serving as a structural indicator.
  • Theoretical models predict thiolate protonation at neutral pH in solution for Cys4-Zn2+ groups.

Conclusions:

  • Thiolate protonation is a plausible phenomenon in zinc proteins, particularly Cys4-Zn2+ sites.
  • While PDB structures often show all-thiolate coordination, this may be stabilized by protein environment.
  • Protonated thiolates could exist in proteins with lower experimental resolution or not in the PDB, as suggested by mass spectrometry.