Model Structures of Helicobacter pylori UreD(H) Domains: A Putative Molecular Recognition Platform
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- 作者：Francesco Musiani ; Matteo Bellucci ; Stefano Ciurli
- 刊名：Journal of Chemical Information and Modeling
- 出版年：2011
- 出版时间：July 25, 2011
- 年：2011
- 卷：51
- 期：7
- 页码：1513-1520
- 全文大小：1110K
- 年卷期：v.51,no.7(July 25, 2011)
- ISSN：1549-960X
文摘
The analysis of the sequence of Helicobacter pylori UreD(H), an accessory protein involved in the activation of urease through the assembly of the Ni2+-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.