Receiver domain of sensor histidine kinase CKI1: Difference between revisions
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'''Receiver domain of sensor histidine kinase CKI1''' (CKI1RD) catalyses the transphosphorylation reaction during hormonal and abiotic signalling in plants. Membrane-bound histidine kinase Cytokinin-independet 1 '''(CKI1)''' is a member of the Multistep phosphorelay '''(MSP)''' signalling pathway in ''Arabidopsis''. CKI1 was found to be constitutively active activator of a cytokinin-like response. Intracellularly located C-terminal CKI1RD is responsible for the recognition of CKI1 downstream signalling partners from family of Arabidopsis histidine-containing phosphotransfer proteins '''(AHP)''' and triggers the cytokinin-like signal transmission. Divalent magnesium ion bound in the active site of CKI1RD is essential for the transphosphorylation reaction. Crystal structure of CKI1RD was determined as magnesium-free and magnesium-bound form. Magnesium binding induces the rearrangement of residues around the active site of CKI1RD, as was determined by both X-ray crystallography and NMR spectroscopy. | '''Receiver domain of sensor histidine kinase CKI1''' (CKI1RD) catalyses the transphosphorylation reaction during hormonal and abiotic signalling in plants. Membrane-bound histidine kinase Cytokinin-independet 1 '''(CKI1)''' is a member of the Multistep phosphorelay '''(MSP)''' signalling pathway in ''Arabidopsis''. CKI1 was found to be constitutively active activator of a cytokinin-like response. Intracellularly located C-terminal CKI1RD is responsible for the recognition of CKI1 downstream signalling partners from family of Arabidopsis histidine-containing phosphotransfer proteins '''(AHP)''' and triggers the cytokinin-like signal transmission. Divalent magnesium ion bound in the active site of CKI1RD is essential for the transphosphorylation reaction. Crystal structure of CKI1RD was determined as magnesium-free and magnesium-bound form. Magnesium binding induces the rearrangement of residues around the active site of CKI1RD, as was determined by both X-ray crystallography and NMR spectroscopy. | ||