6Z9N

Copper transporter OprC

6Z9N の概要

• エントリーDOI: 10.2210/pdb6z9n/pdb
• 関連するPDBエントリー: 6FOK 6FOM
• 分子名称: Putative copper transport outer membrane porin OprC, COPPER (II) ION (3 entities in total)
• 機能のキーワード: copper transporter, tbdt, membrane protein, pseudomonas aeruginosa, oprc
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 317567.37

構造登録者

Bhamidimarri, S.P.,van den Berg, B. (登録日: 2020-06-04, 公開日: 2021-06-30, 最終更新日: 2024-01-24)

主引用文献

Bhamidimarri, S.P.,Young, T.R.,Shanmugam, M.,Soderholm, S.,Basle, A.,Bumann, D.,van den Berg, B.
Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.
Plos Biol., 19:e3001446-e3001446, 2021

PubMed Abstract: Copper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it is still unclear whether and how gram-negative bacteria acquire ionic copper. Here, we show that Pseudomonas aeruginosa OprC is an outer membrane, TonB-dependent transporter that is conserved in many Proteobacteria and which mediates acquisition of both reduced and oxidised ionic copper via an unprecedented CxxxM-HxM metal binding site. Crystal structures of wild-type and mutant OprC variants with silver and copper suggest that acquisition of Cu(I) occurs via a surface-exposed "methionine track" leading towards the principal metal binding site. Together with whole-cell copper quantitation and quantitative proteomics in a murine lung infection model, our data identify OprC as an abundant component of bacterial copper biology that may enable copper acquisition under a wide range of conditions.

PubMed: 34762655
DOI: 10.1371/journal.pbio.3001446

実験手法

X-RAY DIFFRACTION (2.73 Å)