7L22

Structure of chloride soak form of ArrX from Chrysiogenes arsenatis

7L22 の概要

• エントリーDOI: 10.2210/pdb7l22/pdb
• 分子名称: ArrX, SULFATE ION (3 entities in total)
• 機能のキーワード: periplasmic binding protein, signaling protein
• 由来する生物種: Chrysiogenes arsenatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34434.86

構造登録者

Maher, M.J.,Poddar, N. (登録日: 2020-12-16, 公開日: 2021-02-17, 最終更新日: 2023-10-18)

主引用文献

Poddar, N.,Badilla, C.,Maghool, S.,Osborne, T.H.,Santini, J.M.,Maher, M.J.
Structural and Functional Investigation of the Periplasmic Arsenate-Binding Protein ArrX from Chrysiogenes arsenatis .
Biochemistry, 60:465-476, 2021

PubMed Abstract: The anaerobic bacterium respires using the oxyanion arsenate (AsO) as the terminal electron acceptor, where it is reduced to arsenite (AsO) while concomitantly oxidizing various organic (e.g., acetate) electron donors. This respiratory activity is catalyzed in the periplasm of the bacterium by the enzyme arsenate reductase (Arr), with expression of the enzyme controlled by a sensor histidine kinase (ArrS) and a periplasmic-binding protein (PBP), ArrX. Here, we report for the first time, the molecular structure of ArrX in the absence and presence of bound ligand arsenate. Comparison of the ligand-bound structure of ArrX with other PBPs shows a high level of conservation of critical residues for ligand binding by these proteins; however, this suite of PBPs shows different structural alterations upon ligand binding. For ArrX and its homologue AioX (from sp. str. NT-26), which specifically binds arsenite, the structures of the substrate-binding sites in the vicinity of a conserved and critical cysteine residue contribute to the discrimination of binding for these chemically similar ligands.

PubMed: 33538578
DOI: 10.1021/acs.biochem.0c00555

実験手法

X-RAY DIFFRACTION (1.925 Å)