5HBQ

C63D mutant of the rhodanese domain of YgaP

Summary for 5HBQ

• Entry DOI: 10.2210/pdb5hbq/pdb
• Related: 5HBL
• Descriptor: Inner membrane protein YgaP, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: s-nitrosylation, s-sulfhydration, rhodanese, transferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P55734
• Total number of polymer chains: 1
• Total formula weight: 14117.22

Authors

Eichmann, C.,Tzitzilonis, C.,Nakamura, T.,Kwiatkowski, W.,Maslennikov, I.,Choe, S.,Lipton, S.A.,Riek, R. (deposition date: 2016-01-02, release date: 2016-08-10, Last modification date: 2024-01-10)

Primary citation

Eichmann, C.,Tzitzilonis, C.,Nakamura, T.,Kwiatkowski, W.,Maslennikov, I.,Choe, S.,Lipton, S.A.,Riek, R.
S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.
J.Mol.Biol., 428:3737-3751, 2016

PubMed Abstract: S-Nitrosylation is well established as an important post-translational regulator in protein function and signaling. However, relatively little is known about its structural and dynamical consequences. We have investigated the effects of S-nitrosylation on the rhodanese domain of the Escherichia coli integral membrane protein YgaP by NMR, X-ray crystallography, and mass spectrometry. The results show that the active cysteine in the rhodanese domain of YgaP is subjected to two competing modifications: S-nitrosylation and S-sulfhydration, which are naturally occurring in vivo. It has been observed that in addition to inhibition of the sulfur transfer activity, S-nitrosylation of the active site residue Cys63 causes an increase in slow motion and a displacement of helix 5 due to a weakening of the interaction between the active site and the helix dipole. These findings provide an example of how nitrosative stress can exert action at the atomic level.

PubMed: 27473602
DOI: 10.1016/j.jmb.2016.07.010

Experimental method

X-RAY DIFFRACTION (1.66 Å)