5n0k

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Rat ceruloplasmin orthorhombic form

Structural highlights

5n0k is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:CA, CU, NA, NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CERU_RAT Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (By similarity). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (PubMed:14707133). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols. Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (By similarity).[UniProtKB:P00450][1]

Publication Abstract from PubMed

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 A 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 A demonstrates unexpected partial substitution of copper by zinc.

Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.,Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO, Kolmakov NN, Vasilyev VB Metallomics. 2017 Nov 27. doi: 10.1039/c7mt00157f. PMID:29177316[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Mani K, Cheng F, Havsmark B, David S, Fransson LA. Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells. J Biol Chem. 2004 Mar 26;279(13):12918-23. PMID:14707133 doi:10.1074/jbc.M313678200
  2. ↑ Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO, Kolmakov NN, Vasilyev VB. Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic. Metallomics. 2017 Nov 27. doi: 10.1039/c7mt00157f. PMID:29177316 doi:http://dx.doi.org/10.1039/c7mt00157f

Contents


PDB ID 5n0k

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OCA

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