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大肠杆菌外膜蛋白A的另一种拓扑模型。

An alternative topological model for Escherichia coli OmpA.

作者信息

Stathopoulos C

机构信息

Department of Microbiology, University of Texas, Austin 78712, USA.

出版信息

Protein Sci. 1996 Jan;5(1):170-3. doi: 10.1002/pro.5560050122.

Abstract

The current topological model for the Escherichia coli outer membrane protein OmpA predicts eight N-terminal transmembrane segments followed by a long periplasmic tail. Several recent reports have raised serious doubts about the accuracy of this prediction. An alternative OmpA model has been constructed using (1) computer-aided predictions developed specifically to predict topology of bacterial outer membrane porins, (2) the results of two reports that identified sequence homologies between OmpA and other peptidoglycan-associated proteins, and (3) biochemical, immunochemical, and genetic topological data on proteins of the OmpA family provided by numerous previous studies. The new model not only agrees with the varied experimental data concerning OmpA but also provides an improved understanding of the relationship between the structure and the multifunctional role of OmpA in the bacterial outer membrane.

摘要

目前关于大肠杆菌外膜蛋白OmpA的拓扑模型预测其有八个N端跨膜片段,随后是一条长的周质尾巴。最近的几份报告对这一预测的准确性提出了严重质疑。已构建了一种替代的OmpA模型,该模型使用了:(1)专门为预测细菌外膜孔蛋白拓扑结构而开发的计算机辅助预测方法;(2)两份报告的结果,这两份报告确定了OmpA与其他肽聚糖相关蛋白之间的序列同源性;(3)众多先前研究提供的关于OmpA家族蛋白的生化、免疫化学和遗传拓扑数据。新模型不仅与关于OmpA的各种实验数据相符,还增进了人们对OmpA在细菌外膜中的结构与多功能作用之间关系的理解。

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