The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centres

Autor:	P.F. Lindley, Kirill Moshkov, Benjamin D. Bax, Adam Ralph, Vjacheslav Zaitsev, Irina S. Zaitseva, Graeme Card
Rok vydání:	1996
Předmět:	chemistry.chemical_classification Methionine biology Stereochemistry chemistry.chemical_element Biochemistry Copper Inorganic Chemistry chemistry.chemical_compound Residue (chemistry) chemistry Oxidoreductase biology.protein Molecule Ceruloplasmin Histidine Cysteine
Zdroj:	JBIC Journal of Biological Inorganic Chemistry. 1:15-23
ISSN:	1432-1327 0949-8257
Popis:	The X-ray structure of human serum ceruloplasmin has been solved at a resolution of 3.1 A. The structure reveals that the molecule is comprised of six plastocyanin-type domains arranged in a triangular array. There are six copper atoms; three form a trinuclear cluster sited at the interface of domains 1 and 6, and there are three mononuclear sites in domains 2, 4 and 6. Each of the mononuclear coppers is coordinated to a cysteine and two histidine residues, and those in domains 4 and 6 also coordinate to a methionine residue; in domain 2, the methionine is replaced by a leucine residue which may form van der Waals type contacts with the copper. The trinuclear centre and the mononuclear copper in domain 6 form a cluster essentially the same as that found in ascorbate oxidase, strongly suggesting an oxidase role for ceruloplasmin in the plasma.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::fc663b147f5a5b72ac19b868edfbb8b3 https://doi.org/10.1007/s007750050018 Zobrazit plný text záznamu Full text from SpringerLink