using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex利用结构信息变化的phosphotransfer特异性趋化性信号双组份复杂.pdfVIP

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using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex利用结构信息变化的phosphotransfer特异性趋化性信号双组份复杂.pdf

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using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex利用结构信息变化的phosphotransfer特异性趋化性信号双组份复杂

Using Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling Complex 1,2. 1.¤ 1 2 1 Christian H. Bell , Steven L. Porter , Annabel Strawson , David I. Stuart *, Judith P. Armitage * 1 Oxford Centre for Integrative Systems Biology, Department of Biochemistry, University of Oxford, Oxford, United Kingdom, 2 Division of Structural Biology, University of Oxford, Oxford, United Kingdom Abstract Two-component signal transduction pathways comprising histidine protein kinases (HPKs) and their response regulators (RRs) are widely used to control bacterial responses to environmental challenges. Some bacteria have over 150 different two-component pathways, and the specificity of the phosphotransfer reactions within these systems is tightly controlled to prevent unwanted crosstalk. One of the best understood two-component signalling pathways is ˚ the chemotaxis pathway. Here, we present the 1.40 A crystal structure of the histidine-containing phosphotransfer domain of the chemotaxis HPK, CheA3, in complex with its cognate RR, CheY6. A methionine finger on CheY6 that nestles in a hydrophobic pocket in CheA3 was shown to be important for the interaction and was found to only occur in the cognate RRs of CheA , CheY , and CheB . Site-directed mutagenesis of this methionine in combination with two 3 6 2 adjacent residues abolished binding, as s