Adams Jarrett J, Pal Gour, Yam Katherine, Spencer Holly L, Jia Zongchao, Smith Steven P
Department of Biochemistry, Queen's University, Kingston, ON, K7L 3N6, Canada.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):46-8. doi: 10.1107/S1744309104025837. Epub 2004 Oct 16.
The high-affinity calcium-mediated type II cohesin-dockerin interaction is responsible for the attachment of the multi-enzyme cellulose-degrading complex, termed the cellulosome, to the cell surface of the thermophilic anaerobe Clostridium thermocellum. A trimodular 40 kDa complex comprising the SdbA type II cohesin and the the CipA type II dockerin-X module modular pair from the cellulosome of C. thermocellum has been crystallized. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.21, b = 52.34, c = 154.69 A. The asymmetric unit contains one molecule of the protein complex and native and selenomethionine-derivative crystals diffracted to 2.1 and 2.0 A, respectively.
高亲和力的钙介导的II型黏连蛋白-坞蛋白相互作用负责将称为纤维小体的多酶纤维素降解复合物附着到嗜热厌氧菌热纤梭菌的细胞表面。一种由来自热纤梭菌纤维小体的SdbA II型黏连蛋白和CipA II型坞蛋白-X模块模块对组成的40 kDa三模块复合物已结晶。晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 45.21，b = 52.34，c = 154.69 Å。不对称单元包含一个蛋白质复合物分子，天然晶体和硒代甲硫氨酸衍生晶体分别衍射到2.1 Å和2.0 Å。
