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An adjacent positioning of the H box and the ATP-binding domain is found in type I histidine kinase. In type II histidine kinase, the H box is located a relatively larger distance from the ATP-binding domain. 14 Chieri Tomomoriet al. Advances in the three-dimensional structure determination of histidine kinases significantly improved existing knowledge of the role of the His-Asp phosphorelay signal transduction system. Structural data available to date indicate that members of the histidine kinase family are made of structurally conserved building blocks.
Thus, dimer formation is the obligatory requirement for signal transduction in the HAP system. ROLE OF DNA IN EnvZ FUNCTION An interesting aspect of EnvZ-OmpR-mediated osmoregulation is the role of promoter regions of target genes, ompF and ompC, in sequestering OmpR-P out of the reaction system. It has been reported that phosphorylation of OmpR was enhanced in the presence of DNA fragments containing OmpR-Pbinding regions . We reexamined the effect of DNA fragments on EnvZ function and found that the addition of DNA fragments has a negligible effect on OmpR phosphorylation by EnvZc, but dramatically reduces the dephosphorylation of OmpR-P by EnvZc .
It is clear that class I kinase EnvZ and class II kinase CheA share similar building blocks (the ATP-binding domain and the dimerization domain), but exhibit different spatial arrangement of these building blocks, resulting in different phosphotransfer processes. Furthermore, class II kinases acquired an additional regulatory mechanism provided by the dual SH3 domains. More consideration on domain packing is given in the following section. 18 PHOSPHOTRANSFER Chieri Tomomori et al. DOMAIN To date, three-dimensional structures of the phosphotransfer domain of various proteins have been determined [34-41].