DOI

  • Irina Zaitseva
  • Vjacheslav Zaitsev
  • Graeme Card
  • Kirill Moshkov
  • Benjamin Bax
  • Adam Ralph
  • Peter Lindley

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.

Язык оригиналаанглийский
Страницы (с-по)15-23
Число страниц9
ЖурналJournal of Biological Inorganic Chemistry
Том1
Номер выпуска1
DOI
СостояниеОпубликовано - фев 1996

    Предметные области Scopus

  • Биохимия
  • Неорганическая химия

ID: 5545677