7ATH

Crystal structure of UipA

これはPDB形式変換不可エントリーです。

7ATH の概要

• エントリーDOI: 10.2210/pdb7ath/pdb
• 分子名称: UipA, ZINC ION (3 entities in total)
• 機能のキーワード: native, membrane protein, metal binding, metal binding protein
• 由来する生物種: Microbacterium sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21716.44

構造登録者

Bremond, N.,Gallois, N.,Legrand, P.,Chapon, V.,Arnoux, P. (登録日: 2020-10-30, 公開日: 2021-10-06, 最終更新日: 2024-06-19)

主引用文献

Gallois, N.,Alpha-Bazin, B.,Bremond, N.,Ortet, P.,Barakat, M.,Piette, L.,Mohamad Ali, A.,Lemaire, D.,Legrand, P.,Theodorakopoulos, N.,Floriani, M.,Fevrier, L.,Den Auwer, C.,Arnoux, P.,Berthomieu, C.,Armengaud, J.,Chapon, V.
Discovery and characterization of UipA, a uranium- and iron-binding PepSY protein involved in uranium tolerance by soil bacteria.
Isme J, 16:705-716, 2022

PubMed Abstract: Uranium is a naturally occurring radionuclide. Its redistribution, primarily due to human activities, can have adverse effects on human and non-human biota, which poses environmental concerns. The molecular mechanisms of uranium tolerance and the cellular response induced by uranium exposure in bacteria are not yet fully understood. Here, we carried out a comparative analysis of four actinobacterial strains isolated from metal and radionuclide-rich soils that display contrasted uranium tolerance phenotypes. Comparative proteogenomics showed that uranyl exposure affects 39-47% of the total proteins, with an impact on phosphate and iron metabolisms and membrane proteins. This approach highlighted a protein of unknown function, named UipA, that is specific to the uranium-tolerant strains and that had the highest positive fold-change upon uranium exposure. UipA is a single-pass transmembrane protein and its large C-terminal soluble domain displayed a specific, nanomolar binding affinity for UO and Fe. ATR-FTIR and XAS-spectroscopy showed that mono and bidentate carboxylate groups of the protein coordinated both metals. The crystal structure of UipA, solved in its apo state and bound to uranium, revealed a tandem of PepSY domains in a swapped dimer, with a negatively charged face where uranium is bound through a set of conserved residues. This work reveals the importance of UipA and its PepSY domains in metal binding and radionuclide tolerance.

PubMed: 34556817
DOI: 10.1038/s41396-021-01113-7

実験手法

X-RAY DIFFRACTION (2.343 Å)