Shibata N, Inoue T, Fukuhara K, Nagara Y, Kitagawa R, Harada S, Kasai N, Uemura K, Kato K, Yokota A, Kai Y
Department of Applied Chemistry, Faculty of Engineering, Osaka University, Suita, Osaka 565, Japan.
J Biol Chem. 1996 Oct 25;271(43):26449-52. doi: 10.1074/jbc.271.43.26449.
We determined the crystal structure of spinach ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution and found that the enzyme contained two kinds of S, SI and SII, present in equal number and disposed in an orderly way within the Rubisco holoenzyme. The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The orderly disposition of the heterogeneous small subunits in the Rubisco holoenzyme provides accounts of a multigene family of S in plants.
我们通过X射线衍射在1.8埃分辨率下测定了菠菜1,5 - 二磷酸核酮糖羧化酶/加氧酶（Rubisco）的晶体结构，发现该酶含有两种类型的S，即SI和SII，数量相等且在Rubisco全酶中有序排列。电子密度图表明，SI中第56位残基是亮氨酸，而SII中该位置是组氨酸。还有其他残基差异。因此，菠菜Rubisco具有L8SI4SII4亚基结构。Rubisco全酶中异质小亚基的有序排列为植物中S的多基因家族提供了解释。
