Cendron Laura, Seydel Anke, Angelini Alessandro, Battistutta Roberto, Zanotti Giuseppe
Dipartmento di Scienze Chimiche, Istituto de Chimica Biomoleculare del CNR, Università di Padova, Padua, Italy.
J Mol Biol. 2004 Jul 16;340(4):881-9. doi: 10.1016/j.jmb.2004.05.016.
CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of the total residues. Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.
CagZ是由幽门螺杆菌cag致病岛的cagZ基因(HP0526)编码的一种23 kDa蛋白,已被克隆、过表达、纯化并确定了其三维结构。该蛋白由一个紧凑的单一L形结构域组成,由七个α螺旋构成,约占总残基的70%。三维同源性搜索未发现结构同源物,CagZ可被视为一种新蛋白质折叠的代表。无序的C末端尾巴的存在以及分子表面的性质表明,CagZ可能参与效应蛋白与内膜细胞质侧幽门螺杆菌IV型分泌系统的一种或多种组分的相互作用。