5NQN

CU(I)-CSP3 (COPPER STORAGE PROTEIN 3) FROM METHYLOSINUS

5NQN の概要

• エントリーDOI: 10.2210/pdb5nqn/pdb
• 分子名称: CSP3, COPPER (I) ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: copper-binding protein, methane oxidation, copper storage, methanotrophs, particulate methane monooxygenase
• 由来する生物種: Methylosinus trichosporium OB3b
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15521.95

構造登録者

Basle, A.,Platsaki, S.,Dennison, C. (登録日: 2017-04-20, 公開日: 2017-05-31, 最終更新日: 2024-01-17)

主引用文献

Basle, A.,Platsaki, S.,Dennison, C.
Visualizing Biological Copper Storage: The Importance of Thiolate-Coordinated Tetranuclear Clusters.
Angew. Chem. Int. Ed. Engl., 56:8697-8700, 2017

PubMed Abstract: Bacteria possess cytosolic proteins (Csp3s) capable of binding large quantities of copper and preventing toxicity. Crystal structures of a Csp3 plus increasing amounts of Cu provide atomic-level information about how a storage protein loads with metal ions. Many more sites are occupied than Cu equiv added, with binding by twelve central sites dominating. These can form [Cu (S-Cys) ] intermediates leading to [Cu (S-Cys) ] , [Cu (S-Cys) ] , and [Cu (S-Cys) (O-Asn)] clusters. Construction of the five Cu sites at the opening of the bundle lags behind the main core, and the two least accessible sites at the opposite end of the bundle are occupied last. Facile Cu cluster formation, reminiscent of that for inorganic complexes with organothiolate ligands, is largely avoided in biology but is used by proteins that store copper in the cytosol of prokaryotes and eukaryotes, where this reactivity is also key to toxicity.

PubMed: 28504850
DOI: 10.1002/anie.201703107

実験手法

X-RAY DIFFRACTION (1.62 Å)