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4czt

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Revision as of 18:36, 4 August 2016

Crystal structure of the kinase domain of SnRK3.23 At1g30270

Structural highlights

4czt is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4czu, 4d28
Activity:	Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Plant 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

↑ Xu J, Li HD, Chen LQ, Wang Y, Liu LL, He L, Wu WH. A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis. Cell. 2006 Jun 30;125(7):1347-60. PMID:16814720 doi:http://dx.doi.org/S0092-8674(06)00769-0
↑ Li L, Kim BG, Cheong YH, Pandey GK, Luan S. A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in Arabidopsis. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12625-30. Epub 2006 Aug 8. PMID:16895985 doi:http://dx.doi.org/0605129103
↑ Lee SC, Lan WZ, Kim BG, Li L, Cheong YH, Pandey GK, Lu G, Buchanan BB, Luan S. A protein phosphorylation/dephosphorylation network regulates a plant potassium channel. Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15959-64. Epub 2007 Sep 26. PMID:17898163 doi:http://dx.doi.org/0707912104
↑ Cheong YH, Pandey GK, Grant JJ, Batistic O, Li L, Kim BG, Lee SC, Kudla J, Luan S. Two calcineurin B-like calcium sensors, interacting with protein kinase CIPK23, regulate leaf transpiration and root potassium uptake in Arabidopsis. Plant J. 2007 Oct;52(2):223-39. PMID:17922773 doi:http://dx.doi.org/10.1111/j.1365-313X.2007.03236.x
↑ Ho CH, Lin SH, Hu HC, Tsay YF. CHL1 functions as a nitrate sensor in plants. Cell. 2009 Sep 18;138(6):1184-94. doi: 10.1016/j.cell.2009.07.004. PMID:19766570 doi:http://dx.doi.org/10.1016/j.cell.2009.07.004
↑ Hashimoto K, Eckert C, Anschutz U, Scholz M, Held K, Waadt R, Reyer A, Hippler M, Becker D, Kudla J. Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins. J Biol Chem. 2012 Mar 9;287(11):7956-68. doi: 10.1074/jbc.M111.279331. Epub 2012 , Jan 17. PMID:22253446 doi:http://dx.doi.org/10.1074/jbc.M111.279331
↑ Chaves-Sanjuan A, Sanchez-Barrena MJ, Gonzalez-Rubio JM, Moreno M, Ragel P, Jimenez M, Pardo JM, Martinez-Ripoll M, Quintero FJ, Albert A. Structural basis of the regulatory mechanism of the plant CIPK family of protein kinases controlling ion homeostasis and abiotic stress. Proc Natl Acad Sci U S A. 2014 Oct 6. pii: 201407610. PMID:25288725 doi:http://dx.doi.org/10.1073/pnas.1407610111

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4czt"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the kinase domain of SnRK3.23 At1g30270==
 <StructureSection load='4czt' size='340' side='right' caption='[[4czt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4czu|4czu]], [[4d28|4d28]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4czt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4czt RCSB], [http://www.ebi.ac.uk/pdbsum/4czt PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4czt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czt OCA], [http://pdbe.org/4czt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4czt RCSB], [http://www.ebi.ac.uk/pdbsum/4czt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4czt ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4czt" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4czt

From Proteopedia

Revision as of 18:36, 4 August 2016

Crystal structure of the kinase domain of SnRK3.23 At1g30270

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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