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首页> 外文期刊>Protein Science: A Publication of the Protein Society >Prediction of the membrane-spanning beta-strands of the major outer membrane protein of Chlamydia.
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Prediction of the membrane-spanning beta-strands of the major outer membrane protein of Chlamydia.

机译：衣原体主要外膜蛋白的跨膜β链的预测。

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摘要

There is preliminary experimental evidence indicating that the major outer-membrane protein (MOMP) of Chlamydia is a porin. We tested this hypothesis for the MOMP of the mouse pneumonitis serovar of Chlamydia trachomatis using two secondary structure prediction methods. First, an algorithm that calculates the mean hydrophobicity of one side of putative beta-strands predicted the positions of 16 transmembrane segments, a structure common to known porins. Second, outer loops typical of porins were assigned using an artificial neural network trained to predict the topology of bacterial outer-membrane proteins with a predominance of beta-strands. A topology model based on these results locates the four variable domains (VDs) of the MOMP on the outer loops and the five constant domains on beta-strands and the periplasmic turns. This model is consistent with genetic analysis and immunological and biochemical data that indicate the VDs are surface exposed. Furthermore, it shows significant homology with the consensus porin model of the program FORESST, which contrasts a proposed secondary structure against a data set of 349 proteins of known structure. Analysis of the MOMP of other chlamydial species corroborated our predicted model.
机译：初步的实验证据表明衣原体的主要外膜蛋白是孔蛋白。我们使用两种二级结构预测方法对沙眼衣原体小鼠肺炎血清型MOMP的这一假设进行了测试。首先，一种计算推定的β链一侧的平均疏水性的算法预测了16个跨膜片段的位置，这是已知孔蛋白的共同结构。其次，使用人工神经网络分配典型的孔蛋白外环，该人工神经网络经过训练可预测以β链为主的细菌外膜蛋白的拓扑结构。基于这些结果的拓扑模型将MOMP的四个可变域（VD）定位在外环上，将五个恒定域定位在β链和周质匝上。该模型与表明VD表面暴露的遗传分析以及免疫学和生化数据一致。此外，它与FORESST程序的共有孔蛋白模型显示出显着同源性，该模型将拟议的二级结构与已知结构的349种蛋白质的数据集进行了对比。其他衣原体物种的MOMP分析证实了我们的预测模型。

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