The X-ray structure of human serum ceruloplasmin at 3.1 Å

Standard

The X-ray structure of human serum ceruloplasmin at 3.1 Å : Nature of the copper centres. / Zaitseva, Irina; Zaitsev, Vjacheslav; Card, Graeme; Moshkov, Kirill; Bax, Benjamin; Ralph, Adam; Lindley, Peter.

In: Journal of Biological Inorganic Chemistry, Vol. 1, No. 1, 02.1996, p. 15-23.

Research output: Contribution to journal › Article › peer-review

Harvard

Zaitseva, I, Zaitsev, V, Card, G, Moshkov, K, Bax, B, Ralph, A & Lindley, P 1996, 'The X-ray structure of human serum ceruloplasmin at 3.1 Å: Nature of the copper centres', Journal of Biological Inorganic Chemistry, vol. 1, no. 1, pp. 15-23. https://doi.org/10.1007/s007750050018

APA

Zaitseva, I., Zaitsev, V., Card, G., Moshkov, K., Bax, B., Ralph, A., & Lindley, P. (1996). The X-ray structure of human serum ceruloplasmin at 3.1 Å: Nature of the copper centres. Journal of Biological Inorganic Chemistry, 1(1), 15-23. https://doi.org/10.1007/s007750050018

Vancouver

Zaitseva I, Zaitsev V, Card G, Moshkov K, Bax B, Ralph A et al. The X-ray structure of human serum ceruloplasmin at 3.1 Å: Nature of the copper centres. Journal of Biological Inorganic Chemistry. 1996 Feb;1(1):15-23. https://doi.org/10.1007/s007750050018

Author

Zaitseva, Irina ; Zaitsev, Vjacheslav ; Card, Graeme ; Moshkov, Kirill ; Bax, Benjamin ; Ralph, Adam ; Lindley, Peter. / The X-ray structure of human serum ceruloplasmin at 3.1 Å : Nature of the copper centres. In: Journal of Biological Inorganic Chemistry. 1996 ; Vol. 1, No. 1. pp. 15-23.

BibTeX

@article{767fecc405ac40dc90034f7e1669aa2d,

title = "The X-ray structure of human serum ceruloplasmin at 3.1 {\AA}: Nature of the copper centres",

abstract = "The X-ray structure of human serum ceruloplasmin has been solved at a resolution of 3.1 {\AA}. 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.",

keywords = "Ceruloplasmin, Copper oxidase, X-ray structure",

author = "Irina Zaitseva and Vjacheslav Zaitsev and Graeme Card and Kirill Moshkov and Benjamin Bax and Adam Ralph and Peter Lindley",

year = "1996",

month = feb,

doi = "10.1007/s007750050018",

language = "English",

volume = "1",

pages = "15--23",

journal = "Journal of Biological Inorganic Chemistry",

issn = "0949-8257",

publisher = "Springer Nature",

number = "1",

}

RIS

TY - JOUR

T1 - The X-ray structure of human serum ceruloplasmin at 3.1 Å

T2 - Nature of the copper centres

AU - Zaitseva, Irina

AU - Zaitsev, Vjacheslav

AU - Card, Graeme

AU - Moshkov, Kirill

AU - Bax, Benjamin

AU - Ralph, Adam

AU - Lindley, Peter

PY - 1996/2

Y1 - 1996/2

N2 - 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.

AB - 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.

KW - Ceruloplasmin

KW - Copper oxidase

KW - X-ray structure

UR - http://www.scopus.com/inward/record.url?scp=3042958993&partnerID=8YFLogxK

U2 - 10.1007/s007750050018

DO - 10.1007/s007750050018

M3 - Article

VL - 1

SP - 15

EP - 23

JO - Journal of Biological Inorganic Chemistry

JF - Journal of Biological Inorganic Chemistry

SN - 0949-8257

IS - 1

ER -

ID: 5545677