X-ray diffraction study of highly purified human ceruloplasmin
- Russian Academy of Medical Sciences, Institute of Experimental Medicine (Russian Federation)
- Max Planck Unit for Structural Molecular Biology at DESY (Germany)
The three-dimensional structure of ceruloplasmin (CP) with unoccupied labile metal-binding sites and the structure of CP containing Ni{sup 2+} in the labile sites were solved for the first time at 2.6 and 2.95 A resolution, respectively. Crystallization was performed with the use of storage-stable CP, which was prepared in the presence of proteinase inhibitors and purified from (pre)proteinases. Ceruloplasmin with Ni{sup 2+} crystallized in the orthorhombic space group, which had been earlier unknown for CP. Ceruloplasmin with the unoccupied labile sites crystallized in the trigonal crystal form. The differences in intermolecular contacts observed in the trigonal and orthorhombic crystal structures of CP are considered. The conformational changes attendant upon Ni{sup 2+} binding are described. It was suggested that the labile sites are multifunctional and can both bind metal ions potentially toxic to organisms and be involved in electron transfer from substrates to the active site.
- OSTI ID:
- 22050950
- Journal Information:
- Crystallography Reports, Vol. 53, Issue 4; Other Information: Copyright (c) 2008 Pleiades Publishing, Ltd.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
- Country of Publication:
- United States
- Language:
- English
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