4F2E

Crystal structure of the Streptococcus pneumoniae D39 copper chaperone CupA with Cu(I)

4F2E の概要

• エントリーDOI: 10.2210/pdb4f2e/pdb
• 関連するPDBエントリー: 4F2F
• 分子名称: CupA, COPPER (I) ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: cupredoxin fold, cu(i) chaperone, metal transport
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11050.13

構造登録者

Fu, Y.,Dann III, C.E.,Giedroc, D.P. (登録日: 2012-05-07, 公開日: 2013-01-30, 最終更新日: 2024-02-28)

主引用文献

Fu, Y.,Tsui, H.C.,Bruce, K.E.,Sham, L.T.,Higgins, K.A.,Lisher, J.P.,Kazmierczak, K.M.,Maroney, M.J.,Dann, C.E.,Winkler, M.E.,Giedroc, D.P.
A new structural paradigm in copper resistance in Streptococcus pneumoniae.
Nat.Chem.Biol., 9:177-183, 2013

PubMed Abstract: Copper resistance has emerged as an important virulence determinant of microbial pathogens. In Streptococcus pneumoniae, copper resistance is mediated by the copper-responsive repressor CopY, CupA and the copper-effluxing P(1B)-type ATPase CopA. We show here that CupA is a previously uncharacterized cell membrane-anchored Cu(I) chaperone and that a Cu(I) binding-competent, membrane-localized CupA is obligatory for copper resistance. The crystal structures of the soluble domain of CupA and the N-terminal metal-binding domain (MBD) of CopA (CopA(MBD)) reveal isostructural cupredoxin-like folds that each harbor a binuclear Cu(I) cluster unprecedented in bacterial copper trafficking. NMR studies reveal unidirectional Cu(I) transfer from the low-affinity site on the soluble domain of CupA to the high-affinity site of CopA(MBD). However, copper binding by CopA(MBD) is not essential for cellular copper resistance, consistent with a primary role of CupA in cytoplasmic Cu(I) sequestration and/or direct delivery to the transmembrane site of CopA for cellular efflux.

PubMed: 23354287
DOI: 10.1038/nchembio.1168

実験手法

X-RAY DIFFRACTION (1.449 Å)