通过小角X射线散射观察龙虾α-甲壳蓝蛋白的四级结构。
Quaternary structure of alpha-crustacyanin from lobster as seen by small-angle X-ray scattering.
作者信息
Dellisanti Cosma D, Spinelli Silvia, Cambillau Christian, Findlay John B C, Zagalsky Peter F, Finet Stéphanie, Receveur-Bréchot Véronique
机构信息
School of Biochemistry and Molecular Biology, University of Leeds, Mount Preston Street, UK.
出版信息
FEBS Lett. 2003 Jun 5;544(1-3):189-93. doi: 10.1016/s0014-5793(03)00486-1.
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.
首次使用小角X射线散射研究了龙虾（螯龙虾）甲壳中的蓝色类胡萝卜素蛋白α-甲壳蓝蛋白的结构。在本文中，我们确定了这种由八个β-甲壳蓝蛋白异二聚体亚基组成的蛋白质的尺寸。对散射光谱的分析和对α-甲壳蓝蛋白形状的估计表明，该蛋白质可装入一个轴向长度为238埃、半径为47.5埃的圆柱体中，其中八个β-甲壳蓝蛋白分子可能以螺旋方式排列。
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