Structure, of full-length bacterial chitinase containing two fibronectin type III domains revealed by small angle X-ray scattering
Structure, of full-length bacterial chitinase containing two fibronectin type III domains revealed by small angle X-ray scattering
复制标题
DOI：
10.1016/j.bbrc.2006.07.096
复制
发表时间：
2006-09-29
影响因子：
3.1
通讯作者：
Watanabe, Takeshi
中科院分区：
文献类型：
--
作者：
Toratani, Tadayuki;Kezuka, Yulchiro;Watanabe, Takeshi
环状芽孢杆菌WL-12的几丁质酶A1（ChiA 1）由N-末端催化结构域、两个纤连蛋白III型结构域（FnIIID）和C-末端几丁质结合结构域组成。用小角X射线散射研究了ChiA 1的全长结构。低分辨率结构显示ChiA I是一个长形分子，长度约为145埃，由一个大的球形头部和一个棒状尾部组成。结合已知的高分辨率结构的个别ChiA 1域提供了一个模型的域的安排。在该模型中，两个FnIIID以延伸的棒状形状彼此连接，而FnIIID之间没有大的弯曲，并且对ChiA 1的长度有很大贡献。(c)2006年爱思唯尔公司All rights reserved.
Chitinase A1 (ChiA1) from Bacillus circulans WL-12 consists of an N-terminal catalytic domain, two fibronectin type III domains (FnIIIDs), and a C-terminal chitin-binding domain. The full-length structure of ChiA1 was studied by small angle X-ray scattering. The obtained low-resolution structure showed that ChiA I is an elongated molecule with a length of similar to 145 angstrom composed of a large globular head and a rod-like tail. Combination with known high-resolution structures of individual ChiA1 domains provided a model of the domain arrangement. In this model, two FnIIIDs connect to each other in an extended rod-like shape without large bending between the FnIIIDs, and contribute largely to the length of ChiA1. (c) 2006 Elsevier Inc. All rights reserved.