8BWV

Crystal Structure of SilF Cu(I)

8BWV の概要

• エントリーDOI: 10.2210/pdb8bwv/pdb
• 関連するPDBエントリー: 8BBZ 8BHU
• 分子名称: SilF, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: cu(i) metallochaperone, metal binding, metal binding protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 52734.64

構造登録者

Lithgo, R.M.,Carr, S.B.,Scott, D.J.,Quigley, A. (登録日: 2022-12-07, 公開日: 2024-01-24, 最終更新日: 2025-08-06)

主引用文献

Lithgo, R.M.,Hanzevacki, M.,Harris, G.,Kamps, J.J.A.G.,Holden, E.,Gianga, T.M.,Benesch, J.L.P.,Jager, C.M.,Croft, A.K.,Hussain, R.,Hobman, J.L.,Orville, A.M.,Quigley, A.,Carr, S.B.,Scott, D.J.
The adaptability of the ion-binding site by the Ag(I)/Cu(I) periplasmic chaperone SilF.
J.Biol.Chem., 299:105331-105331, 2023

PubMed Abstract: The periplasmic chaperone SilF has been identified as part of an Ag(I) detoxification system in Gram-negative bacteria. Sil proteins also bind Cu(I) but with reported weaker affinity, therefore leading to the designation of a specific detoxification system for Ag(I). Using isothermal titration calorimetry, we show that binding of both ions is not only tighter than previously thought but of very similar affinities. We investigated the structural origins of ion binding using molecular dynamics and QM/MM simulations underpinned by structural and biophysical experiments. The results of this analysis showed that the binding site adapts to accommodate either ion, with key interactions with the solvent in the case of Cu(I). The implications of this are that Gram-negative bacteria do not appear to have evolved a specific Ag(I) efflux system but take advantage of the existing Cu(I) detoxification system. Therefore, there are consequences for how we define a particular metal resistance mechanism and understand its evolution in the environment.

PubMed: 37820867
DOI: 10.1016/j.jbc.2023.105331

実験手法

X-RAY DIFFRACTION (2.2 Å)