Lanmodulin remains unfolded and fails to interact with lanthanide ions in Escherichia coli cells.
Qiong WuXiaoli LiuZhaofei ChaiKai ChengGuohua XuLing JiangMaili LiuConggang LiPublished in: Chemical communications (Cambridge, England) (2022)
We report the conformation of a newly discovered specific lanthanide ion (Ln 3+ ) binding protein, lanmodulin (LanM), and its interaction with Ln 3+ in Escherichia coli cells using the in-cell NMR technique. We found that LanM remains unfolded and fails to bind Ln 3+ in Escherichia coli cells due to the abundance of phosphate groups.
Keyphrases
- escherichia coli
- induced apoptosis
- cell cycle arrest
- endoplasmic reticulum stress
- high resolution
- single molecule
- mass spectrometry
- mesenchymal stem cells
- single cell
- oxidative stress
- cell proliferation
- klebsiella pneumoniae
- quantum dots
- endoplasmic reticulum
- metal organic framework
- crystal structure
- energy transfer