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参与细菌趋化作用的信号蛋白晶格的分子模型。

Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis.

作者信息

Shimizu T S, Le Novère N, Levin M D, Beavil A J, Sutton B J, Bray D

机构信息

[1] Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK.

出版信息

Nat Cell Biol. 2000 Nov;2(11):792-6. doi: 10.1038/35041030.

DOI:10.1038/35041030
PMID:11056533
Abstract

Coliform bacteria detect chemical attractants by means of a membrane-associated cluster of receptors and signalling molecules. We have used recently determined molecular structures, in conjunction with plastic models generated by three-dimensional printer technology, to predict how the proteins of the complex are arranged in relation to the plasma membrane. The proposed structure is a regular two-dimensional lattice in which the cytoplasmic ends of chemotactic-receptor dimers are inserted into a hexagonal array of CheA and CheW molecules. This structure creates separate compartments for adaptation and downstream signalling, and indicates a possible basis for the spread of activity within the cluster.

摘要

大肠菌群通过与膜相关的受体和信号分子簇来检测化学引诱剂。我们最近利用已确定的分子结构,结合三维打印机技术生成的塑料模型,来预测该复合物中的蛋白质相对于质膜是如何排列的。所提出的结构是一种规则的二维晶格,其中趋化受体二聚体的胞质端插入到CheA和CheW分子的六边形阵列中。这种结构为适应和下游信号传导创造了独立的隔室,并表明了簇内活性传播的可能基础。

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