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Background  Plants reprogram metabolism and development to rapidly adapt to biotic and abiotic stress. Protein kinases play a significant role in this process by phosphorylating protein substrates that activate or inactivate signaling cascades that regulate cellular and metabolic adaptations. Despite their importance in plant biology, a notably small fraction of the plant kinomes has been studied to date.    Results  In this report, we describe  Zm DRIK1, a stress-responsive receptor-like pseudokinase whose expression is downregulated under water restriction. We show the structural features and molecular basis of the absence of ATP binding exhibited by  Zm DRIK1. The  Zm DRIK1 kinase domain lacks conserved amino acids that are essential for phosphorylation activity. The crystal structure of the  Zm DRIK1 kinase domain revealed the presence of a spine formed by the side chain of the triad Leu 240 , Tyr 363 , and Leu 375  that occludes the ATP binding pocket. Although  Zm DRIK1 is unable to bind nucleotides, it does bind the small molecule ENMD-2076 which, in a cocrystal structure, revealed the potential to serve as a  Zm DRIK1 inhibitor.    Conclusion   Zm DRIK1 is a novel receptor-like pseudokinase responsive to biotic and abiotic stress. The absence of ATP binding and consequently, the absence of phosphorylation activity, was proven by the crystal structure of the apo form of the protein kinase domain. The expression profiling of the gene encoding  Zm DRIK1 suggests this kinase may play a role in downregulating the expression of stress responsive genes that are not necessary under normal conditions. Under biotic and abiotic stress,  Zm DRIK1 is down-regulated to release the expression of these stress-responsive genes.

Crystal structure of DRIK1, a stress-responsive receptor-like pseudokinase, reveals the molecular basis for the absence of ATP binding