2j5w

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spinqualitylabelsall models 2j5w, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CERULOPLASMIN REVISITED: STRUCTURAL AND FUNCTIONAL ROLES OF VARIOUS METAL CATION BINDING SITES

Overview

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.

About this Structure

2J5W is a Single protein structure of sequence from Homo sapiens with NAG, CA, NA, CU, O, OXY and GOL as ligands. Active as Ferroxidase, with EC number 1.16.3.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites., Bento I, Peixoto C, Zaitsev VN, Lindley PF, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):240-8. Epub 2007, Jan 16. PMID:17242517

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