5N4L

Rat ceruloplasmin trigonal form

5N4L の概要

• エントリーDOI: 10.2210/pdb5n4l/pdb
• 分子名称: Ceruloplasmin, COPPER (II) ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, copper-binding
• 由来する生物種: Rattus norvegicus (Rat)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 236833.36

構造登録者

Samygina, V.R.,Sokolov, A.V.,Bourenkov, G.,Vasilyev, V.B. (登録日: 2017-02-11, 公開日: 2017-12-13, 最終更新日: 2024-11-13)

主引用文献

Samygina, V.R.,Sokolov, A.V.,Bourenkov, G.,Schneider, T.R.,Anashkin, V.A.,Kozlov, S.O.,Kolmakov, N.N.,Vasilyev, V.B.
Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.
Metallomics, 9:1828-1838, 2017

PubMed Abstract: Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 Å resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 Å demonstrates unexpected partial substitution of copper by zinc.

PubMed: 29177316
DOI: 10.1039/c7mt00157f

実験手法

X-RAY DIFFRACTION (3.2 Å)