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S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.

Cédric Eichmann1, Christos Tzitzilonis2, Tomohiro Nakamura3

  • 1Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.

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S-nitrosylation of the YgaP protein

Keywords:
X-ray crystallographymass spectrometrynuclear magnetic resonance (NMR)post-translational modificationrhodanese

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • S-nitrosylation is a key post-translational modification regulating protein function.
  • The structural and dynamic effects of S-nitrosylation are not well understood.

Purpose of the Study:

  • To investigate the impact of S-nitrosylation on the rhodanese domain of E. coli YgaP.
  • To elucidate the structural and dynamical consequences of S-nitrosylation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • X-ray crystallography
  • Mass spectrometry

Main Results:

  • Identified competing S-nitrosylation and S-sulfhydration of the active cysteine (Cys63) in YgaP.
  • S-nitrosylation inhibits sulfur transfer activity.
  • Observed increased slow motion and helix 5 displacement due to weakened active site interactions.

Conclusions:

  • S-nitrosylation of YgaP's active site cysteine alters protein dynamics and structure.
  • Nitrosative stress can induce atomic-level changes in protein function.
  • YgaP rhodanese domain is subject to competing endogenous modifications.