The HBM domain: Introducing bimodularity to bacterial sensing

The HBM domain: Introducing bimodularity to bacterial sensing
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DOI:
10.1002/pro.2410
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发表时间:
2014-03
期刊:
影响因子:
8
通讯作者:
Á. Ortega;T. Krell
Á. Ortega;T. Krell
中科院分区:
生物学3区
文献类型:
--
作者:
Á. Ortega;T. Krell

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我们最近报道了McpS化学受体传感器结构域及其同源配体的三维结构。该结构域具有双模结构,其中配体与每个模块结合引起趋化反应。这是一个新的小分子结合结构域,但是在相关数据库中没有注释。我们在此报告了McpS - like传感器结构域家族的结构域特征,该结构域被称为螺旋双模(HBM)结构域。HBM结构域在细菌和古细菌中被发现,是化学受体和组氨酸激酶的一部分。两个模块的配体结合位点氨基酸的保守性表明HBM家族成员识别相似的配体。
We have recently reported the three dimensional structure of the McpS chemoreceptor sensor domain in complex with its cognate ligands. The domain was characterized by a bimodular architecture, where ligand binding to each module caused a chemotactic response. This is a novel small molecule binding domain, which, however, is un‐annotated in relevant databases. We report here the domain signature of the family of McpS‐like sensor domains, which was termed helical bimodular (HBM) domain. The HBM domain was identified in Bacteria and Archaea and forms part of chemoreceptors and histidine kinases. The conservation of amino acids in the ligand binding sites of both modules suggests that HBM family members recognize similar ligands.