Quaternary structure of alpha‐crustacyanin from lobster as seen by small‐angle X‐ray scattering

The structure of α‐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 β‐crustacyanin...

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Bibliographic Details
Published in:FEBS Letters
Main Authors: Dellisanti, Cosma D, Spinelli, Silvia, Cambillau, Christian, Findlay, John B.C, Zagalsky, Peter F, Finet, Stéphanie, Receveur-Bréchot, Véronique
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2003
Subjects:
Homarus gammarus
Online Access:http://dx.doi.org/10.1016/s0014-5793(03)00486-1
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https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2803%2900486-1
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Summary:The structure of α‐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 β‐crustacyanin. Analysis of the scattering spectra and estimation of the shape of α‐crustacyanin show that the protein fits into a cylinder with an axial length of 238 Å and a radius of 47.5 Å, in which the eight β‐crustacyanin molecules are probably arranged in a helical manner.

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