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2XLA

Structure and metal-loading of a soluble periplasm cupro-protein: Cu- CucA-closed

2XLA の概要
エントリーDOI10.2210/pdb2xla/pdb
関連するPDBエントリー2XL7 2XL9 2XLF 2XLG
分子名称SLL1785 PROTEIN, COPPER (II) ION, UREA, ... (4 entities in total)
機能のキーワードmetal binding protein, cupin
由来する生物種SYNECHOCYSTIS SP. PCC 6803
タンパク質・核酸の鎖数4
化学式量合計108027.81
構造登録者
Waldron, K.J.,Firbank, S.J.,Dainty, S.J.,Perez-Rama, M.,Tottey, S.,Robinson, N.J. (登録日: 2010-07-20, 公開日: 2010-08-11, 最終更新日: 2023-12-20)
主引用文献Waldron, K.J.,Firbank, S.J.,Dainty, S.J.,Perez-Rama, M.,Tottey, S.,Robinson, N.J.
Structure and Metal Loading of a Soluble Periplasm Cuproprotein.
J.Biol.Chem., 285:32504-, 2010
Cited by
PubMed Abstract: A copper-trafficking pathway was found to enable Cu(2+) occupancy of a soluble periplasm protein, CucA, even when competing Zn(2+) is abundant in the periplasm. Here, we solved the structure of CucA (a new cupin) and found that binding of Cu(2+), but not Zn(2+), quenches the fluorescence of Trp(165), which is adjacent to the metal site. Using this fluorescence probe, we established that CucA becomes partly occupied by Zn(2+) following exposure to equimolar Zn(2+) and Cu(2+). Cu(2+)-CucA is more thermodynamically stable than Zn(2+)-CucA but k((Zn→Cu)exchange) is slow, raising questions about how the periplasm contains solely the Cu(2+) form. We discovered that a copper-trafficking pathway involving two copper transporters (CtaA and PacS) and a metallochaperone (Atx1) is obligatory for Cu(2+)-CucA to accumulate in the periplasm. There was negligible CucA protein in the periplasm of ΔctaA cells, but the abundance of cucA transcripts was unaltered. Crucially, ΔctaA cells overaccumulate low M(r) copper complexes in the periplasm, and purified apoCucA can readily acquire Cu(2+) from ΔctaA periplasm extracts, but in vivo apoCucA fails to come into contact with these periplasmic copper pools. Instead, copper traffics via a cytoplasmic pathway that is coupled to CucA translocation to the periplasm.
PubMed: 20702411
DOI: 10.1074/JBC.M110.153080
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.93 Å)
構造検証レポート
Validation report summary of 2xla
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件を2024-10-30に公開中

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