5N4L

Rat ceruloplasmin trigonal form

Summary for 5N4L

• Entry DOI: 10.2210/pdb5n4l/pdb
• Descriptor: Ceruloplasmin, COPPER (II) ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, copper-binding
• Biological source: Rattus norvegicus (Rat)
• Total number of polymer chains: 2
• Total formula weight: 236833.36

Authors

Samygina, V.R.,Sokolov, A.V.,Bourenkov, G.,Vasilyev, V.B. (deposition date: 2017-02-11, release date: 2017-12-13, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)