Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites

Isabel Bento, Cristina Peixoto, Vjacheslav N. Zaitsev, Peter F. Lindley

Research output: Contribution to journalArticlepeer-review

86 Citations (Scopus)

Abstract

The three-dimensional molecular structure of human serum ceruloplasmin has been reinvestigated using X-ray synchrotron data collected at 100 K from a crystal frozen to liquid-nitrogen temperature. The resulting model, with an increase in resolution from 3.1 to 2.8 angstrom, gives an overall improvement of the molecular structure, in particular the side chains. In addition, it enables the clear definition of previously unidentified Ca2+- binding and Na+- binding sites. The Ca2+ cation is located in domain 1 in a configuration very similar to that found in the activated bovine factor Va. The Na+ sites appear to play a structural role in providing rigidity to the three protuberances on the top surface of the molecule. These features probably help to steer substrates towards the mononuclear copper sites prior to their oxidation and to restrict the size of the approaching substrate. The trinuclear copper centre appears to differ from the room-temperature structure in that a dioxygen moiety is bound in a similar way to that found in the endospore coat protein CotA from Bacillus subtilis.

Original languageEnglish
Pages (from-to)240-248
Number of pages9
JournalActa Crystallographica. Section D, Biological crystallography
Volume63
DOIs
Publication statusPublished - Feb 2007

Keywords

  • CRYSTAL-STRUCTURE
  • OXIDASE ACTIVITY
  • FULL COMPLEMENT
  • PROTEIN
  • RESOLUTION
  • LACCASE
  • PLASMA
  • ANGSTROM
  • CHAINS
  • ERRORS

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