4czu

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the kinase domain of CIPK23 T190D mutant

Structural highlights

4czu is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	,
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/4czu"

Categories: Arabidopsis thaliana | Large Structures | Albert A | Chaves-Sanjuan A | Sanchez-Barrena MJ

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4czu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CZU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4czu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czu OCA], [https://pdbe.org/4czu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4czu RCSB], [https://www.ebi.ac.uk/pdbsum/4czu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4czu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CIPKN_ARATH 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.<ref>PMID:16814720</ref> <ref>PMID:16895985</ref> <ref>PMID:17898163</ref> <ref>PMID:17922773</ref> <ref>PMID:19766570</ref> <ref>PMID:22253446</ref>
+[https://www.uniprot.org/uniprot/CIPKN_ARATH 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.<ref>PMID:16814720</ref> <ref>PMID:16895985</ref> <ref>PMID:17898163</ref> <ref>PMID:17922773</ref> <ref>PMID:19766570</ref> <ref>PMID:22253446</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4czu

From Proteopedia

Current revision

Crystal structure of the kinase domain of CIPK23 T190D mutant

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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