6EU7

Structure of the arsenite-bound form of AioX from Rhizobium sp. str. NT-26

6EU7 の概要

• エントリーDOI: 10.2210/pdb6eu7/pdb
• 分子名称: Putative periplasmic phosphite-binding-like protein (Pbl) PtxB-like protein designated AioX (2 entities in total)
• 機能のキーワード: periplasmic-binding protein, arsenic, arsenite-binding, rhizobium nt-26, signaling protein
• 由来する生物種: Rhizobium sp. NT-26
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 187519.18

構造登録者

Djordjevic, S.,Badilla, C.,Cole, A.,Santini, J. (登録日: 2017-10-28, 公開日: 2018-10-17, 最終更新日: 2024-11-13)

主引用文献

Badilla, C.,Osborne, T.H.,Cole, A.,Watson, C.,Djordjevic, S.,Santini, J.M.
A new family of periplasmic-binding proteins that sense arsenic oxyanions.
Sci Rep, 8:6282-6282, 2018

PubMed Abstract: Arsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that's role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate.

PubMed: 29674678
DOI: 10.1038/s41598-018-24591-w

実験手法

X-RAY DIFFRACTION (3 Å)