The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY.

摘要: To structurally characterize the activated state of transiently phosphorylated signal transduction protein CheY, we have constructed an α-thiophosphonate derivative CheY D57C point mutant and determined its three-dimensional structure at 1.85 A resolution. We also characterized this analogue with high-resolution NMR studied binding to a peptide derived from FliM, CheY's target component flagellar motor. The chemically modified derivative, phosphono-CheY, exhibits many chemical properties wild-type except that it is indefinitely stable. Electron density for substitution clear readily interpretable; omit refinement phosphorus atom greater than 10σ. molecule shows number localized conformational changes are believed constitute postphosphorylation activation events. most obvious these include movement side chain active site base, Lys 109, predomin...