Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation-binding Sites

Overview

Journal Acta Crystallogr D Biol Crystallogr

Specialty Chemistry

Date 2007 Jan 24

PMID 17242517

Citations 48

Authors

Isabel Bento

Cristina Peixoto

Vjacheslav N Zaitsev

Peter F Lindley

Affiliations

Soon will be listed here.

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 A, 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.

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