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

FEBS Letters

Finet, Stéphanie¹  Cambillau, Christian⁴  Dellisanti, Cosma D²  Receveur-Bréchot, Véronique⁴  Spinelli, Silvia⁴  Findlay, John B.C²  Zagalsky, Peter F³ 

[1] European Synchrotron Radiation Facility, BP 220, 38043 Grenoble Cedex, France;School of Biochemistry and Molecular Biology, University of Leeds, Mount Preston Street, Leeds LS2 9JT, UK;School of Biological Sciences, Royal Holloway College, University of London, Egham Hill, Egham TW20 0EX, UK;Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France

关键词: Small-angle X-ray scattering;    Carotenoprotein;    Lipocalin;    Quaternary structure;   

DOI  :  10.1016/S0014-5793(03)00486-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown