4czu
From Proteopedia
Crystal structure of the kinase domain of SnRK3.23 At1g30270 T190D mutant
Structural highlights
Function[CIPKN_ARATH] CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein leads to activation of the kinase in a calcium-dependent manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by phosphorylation the K(+) conductance and uptake of AKT1 in low K(+) condition, in response to calcium signaling and during the stomatal opening regulation by monitoring the turgor pressure in guard cells. In response to low nitrate concentration, phosphorylates NRT1.1, switching it from a low-affinity nitrate transporter to a high-affinity transporter. Confers tolerance to low potassium conditions. Involved in drought sensitivity and leaf transpiration.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedPlant cells have developed specific protective molecular machinery against environmental stresses. The family of CBL-interacting protein kinases (CIPK) and their interacting activators, the calcium sensors calcineurin B-like (CBLs), work together to decode calcium signals elicited by stress situations. The molecular basis of biological activation of CIPKs relies on the calcium-dependent interaction of a self-inhibitory NAF motif with a particular CBL, the phosphorylation of the activation loop by upstream kinases, and the subsequent phosphorylation of the CBL by the CIPK. We present the crystal structures of the NAF-truncated and pseudophosphorylated kinase domains of CIPK23 and CIPK24/SOS2. In addition, we provide biochemical data showing that although CIPK23 is intrinsically inactive and requires an external stimulation, CIPK24/SOS2 displays basal activity. This data correlates well with the observed conformation of the respective activation loops: Although the loop of CIPK23 is folded into a well-ordered structure that blocks the active site access to substrates, the loop of CIPK24/SOS2 protrudes out of the active site and allows catalysis. These structures together with biochemical and biophysical data show that CIPK kinase activity necessarily requires the coordinated releases of the activation loop from the active site and of the NAF motif from the nucleotide-binding site. Taken all together, we postulate the basis for a conserved calcium-dependent NAF-mediated regulation of CIPKs and a variable regulation by upstream kinases. Structural basis of the regulatory mechanism of the plant CIPK family of protein kinases controlling ion homeostasis and abiotic stress.,Chaves-Sanjuan A, Sanchez-Barrena MJ, Gonzalez-Rubio JM, Moreno M, Ragel P, Jimenez M, Pardo JM, Martinez-Ripoll M, Quintero FJ, Albert A Proc Natl Acad Sci U S A. 2014 Oct 6. pii: 201407610. PMID:25288725[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||||
