5LAM

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

5LAM の概要

• エントリーDOI: 10.2210/pdb5lam/pdb
• 関連するPDBエントリー: 2MOI
• NMR情報: BMRB: 34009
• 分子名称: Inner membrane protein YgaP (1 entity in total)
• 機能のキーワード: rhodanese domain of ygap, protein, membrane protein
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11716.31

構造登録者

Eichmann, C.,Tzitzilonis, C.,Nakamura, T.,Maslennikov, I.,Kwiatkowski, W.,Choe, S.,Lipton, S.A.,Guntert, P.,Riek, R. (登録日: 2016-06-14, 公開日: 2016-08-17, 最終更新日: 2024-06-19)

主引用文献

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

実験手法

SOLUTION NMR