期刊
PROTEIN SCIENCE
卷 23, 期 3, 页码 332-336出版社
WILEY
DOI: 10.1002/pro.2410
关键词
domain profile; chemotaxis receptor; histidine kinase; sequence analysis
资金
- European Union through Junta de Andalucia [P09-RNM-4509, CVI-7335]
- Spanish Ministry of Economy and Competitiveness [Bio2010-16937]
- CSIC
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.
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