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首页> 美国卫生研究院文献>Molecules >New Insights on the Feature and Function of Tail Tubular Protein B and Tail Fiber Protein of the Lytic Bacteriophage φYeO3-12 Specific for
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New Insights on the Feature and Function of Tail Tubular Protein B and Tail Fiber Protein of the Lytic Bacteriophage φYeO3-12 Specific for

机译：新见解关于尾管蛋白B和尾纤维蛋白的特征和功能φYeo3-12特异性

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摘要

For the first time, we are introducing TTPBgp12 and TFPgp17 as new members of the tail tubular proteins B (TTPB) and tail fiber proteins (TFP) family, respectively. These proteins originate from Yersinia enterocolitica phage φYeO3-12. It was originally thought that these were structural proteins. However, our results show that they also inhibit bacterial growth and biofilm formation. According to the bioinformatic analysis, TTPBgp12 is functionally and structurally similar to the TTP of Enterobacteria phage T7 and adopts a β-structure. TFPgp17 contains an intramolecular chaperone domain at its C-terminal end. The N-terminus of TFPgp17 is similar to other representatives of the TFP family. Interestingly, the predicted 3D structure of TFPgp17 is similar to other bacterial S-layer proteins. Based on the thermal unfolding experiment, TTPBgp12 seems to be a two-domain protein that aggregates in the presence of sugars such as maltose and N-acetylglucosamine (GlcNAc). These sugars cause two unfolding events to transition into one global event. TFPgp17 is a one-domain protein. Maltose and GlcNAc decrease the aggregation temperature of TFPgp17, while the presence of N-acetylgalactosamine (GalNAc) increases the temperature of its aggregation. The thermal unfolding analysis of the concentration gradient of TTPBgp12 and TFPgp17 indicates that with decreasing concentrations, both proteins increase in stability. However, a decrease in the protein concentration also causes an increase in its aggregation, for both TTPBgp12 and TFPgp17.
机译：我们首次推出TTPBGP12和TFPGP17作为尾部管状蛋白B（TTPB）和尾纤蛋白（TFP）家族的新成员。这些蛋白质源自yersinia Enterocolitica噬菌体φyeO3-12。最初认为这些是结构蛋白质。然而，我们的结果表明，它们还抑制细菌生长和生物膜形成。根据生物信息分析，TTPBGP12在功能上和结构上类似于肠杆菌噬菌体T7的TTP并采用β结构。 TFPGP17在其C末端含有分子内伴域域。 TFPGP17的N-末端类似于TFP家族的其他代表。有趣的是，TFPGP17的预测3D结构类似于其他细菌S层蛋白。基于热展开实验，TTPBGP12似乎是两层域蛋白，其在存在糖的存在下聚集，例如麦芽糖和N-乙酰葡糖胺（GlcNAc）。这些糖会导致两个展开事件转换为一个全球事件。 TFPGP17是一种单域蛋白。麦芽糖和GLCNAC降低TFPGP17的聚集温度，而N-乙酰甘油蛋胺（GALNAC）的存在增加了其聚集的温度。 TTPBGP12和TFPGP17的浓度梯度的热展开分析表明，随着浓度的降低，蛋白质的稳定性增加。然而，蛋白质浓度的降低也导致TTPBGP12和TFPGP17的聚集增加。

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