2MOL

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

2MOL の概要

• エントリーDOI: 10.2210/pdb2mol/pdb
• 関連するPDBエントリー: 2moi 2moj
• NMR情報: BMRB: 19946
• 分子名称: Inner membrane protein YgaP (1 entity in total)
• 機能のキーワード: rhodanese domain of ygap, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P55734
• 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.,Bordignon, E.,Maslennikov, I.,Choe, S.,Riek, R. (登録日: 2014-04-27, 公開日: 2014-06-25, 最終更新日: 2024-05-15)

主引用文献

Eichmann, C.,Tzitzilonis, C.,Bordignon, E.,Maslennikov, I.,Choe, S.,Riek, R.
Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli.
J.Biol.Chem., 289:23482-23503, 2014

PubMed Abstract: The solution NMR structure of the α-helical integral membrane protein YgaP from Escherichia coli in mixed 1,2-diheptanoyl-sn-glycerol-3-phosphocholine/1-myristoyl-2-hydroxy-sn-glycero-3-phospho-(1'-rac-glycerol) micelles is presented. In these micelles, YgaP forms a homodimer with the two transmembrane helices being the dimer interface, whereas the N-terminal cytoplasmic domain includes a rhodanese-fold in accordance to its sequence homology to the rhodanese family of sulfurtransferases. The enzymatic sulfur transfer activity of full-length YgaP as well as of the N-terminal rhodanese domain only was investigated performing a series of titrations with sodium thiosulfate and potassium cyanide monitored by NMR and EPR. The data indicate the thiosulfate concentration-dependent addition of several sulfur atoms to the catalytic Cys-63, which process can be reversed by the addition of potassium cyanide. The catalytic reaction induces thereby conformational changes within the rhodanese domain, as well as on the transmembrane α-helices of YgaP. These results provide insights into a potential mechanism of YgaP during the catalytic thiosulfate activity in vivo.

PubMed: 24958726
DOI: 10.1074/jbc.M114.571935

実験手法

SOLUTION NMR