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4n0g

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Revision as of 09:50, 5 August 2016

Crystal Structure of PYL13-PP2CA complex

Structural highlights

4n0g is a 4 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	PP2CA, AHG3, At3g11410, F24K9.8 (ARATH), PYL13, RCAR7, At4g18620, F28A21.30 (ARATH)
Activity:	Phosphoprotein phosphatase, with EC number 3.1.3.16
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[P2C37_ARATH] Major negative regulator of abscisic acid (ABA) responses during seed germination and cold acclimation. Confers insensitivity to ABA. Modulates negatively the AKT2/3 activity, which mediates K(+) transport and membrane polarization during stress situations, probably by dephosphorylation. Prevent stomata closure by inactivating the S-type anion efflux channel SLAC1 and its activator SRK2E.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] [PYL13_ARATH] Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA (By similarity).

Publication Abstract from PubMed

PYR1/PYL/RCAR family proteins (PYLs) are well-characterized abscisic acid (ABA) receptors. Among the 14 PYL members in Arabidopsis thaliana, PYL13 is ABA irresponsive and its function has remained elusive. Here, we show that PYL13 selectively inhibits the phosphatase activity of PP2CA independent of ABA. The crystal structure of PYL13-PP2CA complex, which was determined at 2.4 A resolution, elucidates the molecular basis for the specific recognition between PP2CA and PYL13. In addition to the canonical interactions between PYLs and PP2Cs, an extra interface is identified involving an element in the vicinity of a previously uncharacterized CCCH zinc-finger (ZF) motif in PP2CA. Sequence blast identified another 56 ZF-containing PP2Cs, all of which are from plants. The structure also reveals the molecular determinants for the ABA irresponsiveness of PYL13. Finally, biochemical analysis suggests that PYL13 may hetero-oligomerize with PYL10. These two PYLs antagonize each other in their respective ABA-independent inhibitions of PP2Cs. The biochemical and structural studies provide important insights into the function of PYL13 in the stress response of plant and set up a foundation for future biotechnological applications of PYL13.Cell Research advance online publication 29 October 2013; doi:10.1038/cr.2013.143.

Molecular basis for the selective and ABA-independent inhibition of PP2CA by PYL13.,Li W, Wang L, Sheng X, Yan C, Zhou R, Hang J, Yin P, Yan N Cell Res. 2013 Oct 29. doi: 10.1038/cr.2013.143. PMID:24165892^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sheen J. Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants. Proc Natl Acad Sci U S A. 1998 Feb 3;95(3):975-80. PMID:9448270
↑ Tahtiharju S, Palva T. Antisense inhibition of protein phosphatase 2C accelerates cold acclimation in Arabidopsis thaliana. Plant J. 2001 May;26(4):461-70. PMID:11439132
↑ Cherel I, Michard E, Platet N, Mouline K, Alcon C, Sentenac H, Thibaud JB. Physical and functional interaction of the Arabidopsis K(+) channel AKT2 and phosphatase AtPP2CA. Plant Cell. 2002 May;14(5):1133-46. PMID:12034902
↑ Yoshida T, Nishimura N, Kitahata N, Kuromori T, Ito T, Asami T, Shinozaki K, Hirayama T. ABA-hypersensitive germination3 encodes a protein phosphatase 2C (AtPP2CA) that strongly regulates abscisic acid signaling during germination among Arabidopsis protein phosphatase 2Cs. Plant Physiol. 2006 Jan;140(1):115-26. Epub 2005 Dec 9. PMID:16339800 doi:10.1104/pp.105.070128
↑ Kuhn JM, Boisson-Dernier A, Dizon MB, Maktabi MH, Schroeder JI. The protein phosphatase AtPP2CA negatively regulates abscisic acid signal transduction in Arabidopsis, and effects of abh1 on AtPP2CA mRNA. Plant Physiol. 2006 Jan;140(1):127-39. Epub 2005 Dec 16. PMID:16361522 doi:http://dx.doi.org/pp.105.070318
↑ Nishimura N, Yoshida T, Kitahata N, Asami T, Shinozaki K, Hirayama T. ABA-Hypersensitive Germination1 encodes a protein phosphatase 2C, an essential component of abscisic acid signaling in Arabidopsis seed. Plant J. 2007 Jun;50(6):935-49. Epub 2007 Apr 25. PMID:17461784 doi:http://dx.doi.org/10.1111/j.1365-313X.2007.03107.x
↑ Lee SC, Lan W, Buchanan BB, Luan S. A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signaling in plant guard cells. Proc Natl Acad Sci U S A. 2009 Dec 15;106(50):21419-24. doi:, 10.1073/pnas.0910601106. Epub 2009 Dec 2. PMID:19955427 doi:http://dx.doi.org/10.1073/pnas.0910601106
↑ Li W, Wang L, Sheng X, Yan C, Zhou R, Hang J, Yin P, Yan N. Molecular basis for the selective and ABA-independent inhibition of PP2CA by PYL13. Cell Res. 2013 Oct 29. doi: 10.1038/cr.2013.143. PMID:24165892 doi:http://dx.doi.org/10.1038/cr.2013.143

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n0g"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of PYL13-PP2CA complex==
 <StructureSection load='4n0g' size='340' side='right' caption='[[4n0g]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PP2CA, AHG3, At3g11410, F24K9.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), PYL13, RCAR7, At4g18620, F28A21.30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=4n0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n0g RCSB], [http://www.ebi.ac.uk/pdbsum/4n0g 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=4n0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0g OCA], [http://pdbe.org/4n0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n0g RCSB], [http://www.ebi.ac.uk/pdbsum/4n0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0g 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 4n0g" style="background-color:#fffaf0;"></div>
 ==See Also==

4n0g

From Proteopedia

Revision as of 09:50, 5 August 2016

Crystal Structure of PYL13-PP2CA complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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