5LAO

S-nitrosylated 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli

Summary for 5LAO

• Entry DOI: 10.2210/pdb5lao/pdb
• NMR Information: BMRB: 34010
• Descriptor: Inner membrane protein YgaP (1 entity in total)
• Functional Keywords: s-nitrosylated rhodanese domain of ygap, protein, membrane protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 11716.31

Authors

Eichmann, C.,Tzitzilonis, C.,Nakamura, T.,Maslennikov, I.,Kwiatkowski, W.,Choe, S.,Lipton, S.A.,Guntert, P.,Riek, R. (deposition date: 2016-06-14, release date: 2016-08-17, Last modification date: 2024-06-19)

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

SOLUTION NMR