2MRM

Solution structure of the rhodanese domain of YgaP from E. coli

2MRM の概要

• エントリーDOI: 10.2210/pdb2mrm/pdb
• NMR情報: BMRB: 25085
• 分子名称: Membrane protein (1 entity in total)
• 機能のキーワード: rhodanese domain, ygap, e. coli, integral membrane protein, membrane protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12620.39

構造登録者

Wang, W.,Zhou, P.,Tian, C.,Wu, F. (登録日: 2014-07-12, 公開日: 2014-10-08, 最終更新日: 2024-05-01)

主引用文献

Wang, W.,Zhou, P.,He, Y.,Yu, L.,Xiong, Y.,Tian, C.,Wu, F.
Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP
Biochem.Biophys.Res.Commun., 452:817-821, 2014

PubMed Abstract: Rhodanese domains are abundant structural modules that catalyze the transfer of a sulfur atom from thiolsulfates to cyanide via formation of a covalent persulfide intermediate that is bound to an essential conserved cysteine residue. In this study, the three-dimensional structure of the rhodanese domain of YgaP from Escherichia coli was determined using solution NMR. A typical rhodanese domain fold was observed, as expected from the high homology with the catalytic domain of other sulfur transferases. The initial sulfur-transfer step and formation of the rhodanese persulfide intermediate were monitored by addition of sodium thiosulfate using two-dimensional (1)H-(15)N correlation spectroscopy. Discrete sharp signals were observed upon substrate addition, indicting fast exchange between sulfur-free and persulfide-intermediate forms. Residues exhibiting pronounced chemical shift changes were mapped to the structure, and included both substrate binding and surrounding residues.

PubMed: 25204500
DOI: 10.1016/j.bbrc.2014.09.002

実験手法

SOLUTION NMR