Zaitseva, Irina, Zaitsev, Vjacheslav, Card, Graeme, Moshkov, Kirill, Bax, Benjamin  ORCID: https://orcid.org/0000-0003-1940-3785, Ralph, Adam and Lindley, Peter
1996.
The X-ray structure of human serum ceruloplasmin at 3.1.Å: nature of the copper centres.
JBIC Journal of Biological Inorganic Chemistry
1
(1)
, pp. 15-23.
10.1007/s007750050018
|
Abstract
The X-ray structure of human serum ceruloplasmin has been solved at a resolution of 3.1 Å. 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.
| Item Type: | Article |
|---|---|
| Date Type: | Publication |
| Status: | Published |
| Schools: | Schools > Biosciences |
| Publisher: | Springer |
| ISSN: | 0949-8257 |
| Last Modified: | 23 Oct 2022 14:03 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/112645 |
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