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Quaternary structure of alpha-crustacyanin from lobster as seen by small-angle X-ray scattering
Cosma D Dellisanti1, Silvia Spinelli, Christian Cambillau
1School of Biochemistry and Molecular Biology, University of Leeds, Mount Preston Street, UK.
FEBS Letters
|June 5, 2003
Abstract:
The structure of alpha-crustacyanin, the blue carotenoprotein of lobster (Homarus gammarus) carapace, has been investigated for the first time using small-angle X-ray scattering. In this paper, we have determined the dimensions of this protein composed of eight heterodimeric subunits of beta-crustacyanin. Analysis of the scattering spectra and estimation of the shape of alpha-crustacyanin show that the protein fits into a cylinder with an axial length of 238 A and a radius of 47.5 A, in which the eight beta-crustacyanin molecules are probably arranged in a helical manner.