Laboratory of Bioinorganic Chemistry, University of Bologna, Viale G. Fanin 40, 40127 Bologna, Italy.
J Chem Inf Model. 2011 Jul 25;51(7):1513-20. doi: 10.1021/ci200183n. Epub 2011 Jun 13.
The analysis of the sequence of Helicobacter pylori UreD(H), an accessory protein involved in the activation of urease through the assembly of the Ni(2+)-containing active site, revealed the presence of two domains. The structure of these domains was calculated using threading and modeling algorithms. A search for putative binding sites on the protein surface was carried out using dedicated algorithms sensitive to either sequence conservation or structural similarity based on geometry and physicochemical properties. The results suggest that UreD(H) acts as a multifunctional molecular recognition platform facilitating the interaction between apo-urease and the ancillary proteins UreG, UreF, and UreE, responsible for nickel trafficking and delivering.
对参与通过组装含镍活性位点来激活脲酶的辅助蛋白幽门螺杆菌 UreD（H）的序列进行分析，揭示了其存在两个结构域。这些结构域的结构使用穿线和建模算法进行了计算。使用专门的算法，根据几何形状和物理化学性质，对蛋白质表面上的潜在结合位点进行了搜索，这些算法对基于序列保守性或结构相似性的敏感。结果表明，UreD（H）作为一种多功能分子识别平台，促进了脱辅基脲酶与辅助蛋白 UreG、UreF 和 UreE 之间的相互作用，这些蛋白负责镍的运输和递呈。
