Svergun D I, Bećirević A, Schrempf H, Koch M H, Grüber G
European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Biochemistry. 2000 Sep 5;39(35):10677-83. doi: 10.1021/bi000865p.
The shape and overall dimensions of the recently discovered Streptomyces alpha-chitin-binding protein, CHB1, were investigated by synchrotron radiation X-ray solution scattering. The radius of gyration and the maximum size of CHB1 were determined to be 1.75 +/- 0.03 nm and 6.0 +/- 0.2 nm, respectively. Using two independent ab initio approaches the low-resolution shape of the protein was found to consist of two domains, an elongated main globule with a length of about 4 nm and a foot-like domain of about 2 nm width. The structural and functional properties of CHB1 depend strongly on the presence of disulfide bonds; upon their reduction, the protein loses its affinity to chitin.
通过同步辐射X射线溶液散射研究了最近发现的链霉菌α-几丁质结合蛋白CHB1的形状和整体尺寸。CHB1的回转半径和最大尺寸分别确定为1.75±0.03纳米和6.0±0.2纳米。使用两种独立的从头计算方法，发现该蛋白的低分辨率形状由两个结构域组成，一个长度约为4纳米的细长主球体和一个宽度约为2纳米的足状结构域。CHB1的结构和功能特性强烈依赖于二硫键的存在；二硫键还原后，该蛋白失去对几丁质的亲和力。
