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| | ==NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis== | | ==NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis== |
| - | <StructureSection load='1mzk' size='340' side='right' caption='[[1mzk]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1mzk' size='340' side='right'caption='[[1mzk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1mzk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MZK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1mzk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZK FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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'>[https://proteopedia.org/fgij/fg.htm?mol=1mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzk OCA], [https://pdbe.org/1mzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzk RCSB], [https://www.ebi.ac.uk/pdbsum/1mzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzk ProSAT]</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=1mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzk OCA], [http://pdbe.org/1mzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mzk RCSB], [http://www.ebi.ac.uk/pdbsum/1mzk PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/P2C70_ARATH P2C70_ARATH]] Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5 (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1). Functions as a negative regulator of the CLV1 signaling in plant development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1 receptor kinase on threonine residues in the A-loop. Dephosphorylation of SERK1 controls SERK1 internalization (PubMed:12101128). Component of a signaling pathway which mediates adaptation to NaCl stress. Is not a component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).<ref>PMID:12101128</ref> <ref>PMID:15592873</ref> <ref>PMID:18162596</ref> <ref>PMID:9294234</ref> <ref>PMID:9701578</ref> | + | [https://www.uniprot.org/uniprot/P2C70_ARATH P2C70_ARATH] Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5 (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1). Functions as a negative regulator of the CLV1 signaling in plant development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1 receptor kinase on threonine residues in the A-loop. Dephosphorylation of SERK1 controls SERK1 internalization (PubMed:12101128). Component of a signaling pathway which mediates adaptation to NaCl stress. Is not a component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).<ref>PMID:12101128</ref> <ref>PMID:15592873</ref> <ref>PMID:18162596</ref> <ref>PMID:9294234</ref> <ref>PMID:9701578</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mzk_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mzk_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mzk ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Phosphoprotein phosphatase]] | + | [[Category: Large Structures]] |
| - | [[Category: Ding, Z]] | + | [[Category: Ding Z]] |
| - | [[Category: Doren, S R.Van]]
| + | [[Category: Lee G]] |
| - | [[Category: Lee, G]] | + | [[Category: Van Doren SR]] |
| - | [[Category: Walker, J C]] | + | [[Category: Walker JC]] |
| - | [[Category: Beta sandwich]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
P2C70_ARATH Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5 (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1). Functions as a negative regulator of the CLV1 signaling in plant development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1 receptor kinase on threonine residues in the A-loop. Dephosphorylation of SERK1 controls SERK1 internalization (PubMed:12101128). Component of a signaling pathway which mediates adaptation to NaCl stress. Is not a component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Forkhead-associated (FHA) domains are phosphoprotein-binding modules found in diverse signaling proteins that bind partners phosphorylated on threonine or serine. Kinase-associated protein phosphatase from Arabidopsis employs its FHA domain for negative regulation of receptor-like kinase signaling pathways, which are important in plant development. The solution structure of the free state of kinase-interacting FHA domain (KI-FHA) of kinase-associated protein phosphatase has been determined with high precision and accuracy using residual dipolar couplings. KI-FHA is a sandwich of a five-stranded mixed beta-sheet with a six-stranded antiparallel beta-sheet. Despite homology only in the recognition loops, this fold is shared with FHA domains from checkpoint proteins from yeast and humans, as well as with nonhomologous MH2 domains of Smad tumor suppressors. A shared pattern of hydrophobicity throughout FHA domains and Smad MH2 domains may stabilize the core of the beta-sandwich. Evolutionary trace analysis of FHA domains suggests class-specific residues in the recognition loops that could tune their phosphoprotein-binding specificity. This surface agrees with that of KI-FHA in contact with a phosphothreonine peptide ligand. Evolutionary trace analysis also predicts an unexpected swath of class-specific residues on another face of FHA domains. Protein interactions with these faces may affect assembly of transmembrane signaling complexes in plants, and in other FHA domain-containing assemblies.
NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.,Lee GI, Ding Z, Walker JC, Van Doren SR Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:14500786[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shah K, Russinova E, Gadella TW Jr, Willemse J, De Vries SC. The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1. Genes Dev. 2002 Jul 1;16(13):1707-20. PMID:12101128 doi:http://dx.doi.org/10.1101/gad.220402
- ↑ Rienties IM, Vink J, Borst JW, Russinova E, de Vries SC. The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP. Planta. 2005 Jun;221(3):394-405. Epub 2004 Dec 9. PMID:15592873 doi:http://dx.doi.org/10.1007/s00425-004-1447-7
- ↑ Manabe Y, Bressan RA, Wang T, Li F, Koiwa H, Sokolchik I, Li X, Maggio A. The Arabidopsis kinase-associated protein phosphatase regulates adaptation to Na+ stress. Plant Physiol. 2008 Feb;146(2):612-22. Epub 2007 Dec 27. PMID:18162596 doi:http://dx.doi.org/10.1104/pp.107.109009
- ↑ Williams RW, Wilson JM, Meyerowitz EM. A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway. Proc Natl Acad Sci U S A. 1997 Sep 16;94(19):10467-72. PMID:9294234
- ↑ Stone JM, Trotochaud AE, Walker JC, Clark SE. Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions Plant Physiol. 1998 Aug;117(4):1217-25. PMID:9701578
- ↑ Lee GI, Ding Z, Walker JC, Van Doren SR. NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase. Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:14500786 doi:10.1073/pnas.2031918100
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