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| | ==Structure of the BSK8 kinase domain== | | ==Structure of the BSK8 kinase domain== |
| - | <StructureSection load='4i92' size='340' side='right' caption='[[4i92]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4i92' size='340' side='right'caption='[[4i92]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I92 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i92]] is a 1 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=4I92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I92 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i93|4i93]], [[4i94|4i94]]</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=4i92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i92 OCA], [https://pdbe.org/4i92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i92 RCSB], [https://www.ebi.ac.uk/pdbsum/4i92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i92 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g41260, K1O13.5 ([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/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=4i92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i92 OCA], [http://pdbe.org/4i92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i92 RCSB], [http://www.ebi.ac.uk/pdbsum/4i92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i92 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BSK8_ARATH BSK8_ARATH] Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Functions redundantly with BSK3, BSK4, BSK6 and BSK7 (PubMed:23496207). Involved in the regulation of sucrose-phosphate synthase 1 (SPS1) in the context of sucrose resuply after starvation. Activates BSL2, a phosphatase that may dephosphorylate SPS1, leading to the activation of SPS1 (PubMed:24924143).<ref>PMID:23496207</ref> <ref>PMID:24924143</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4i92" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4i92" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Pseudoenzyme|Pseudoenzyme]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Gruetter, C]] | + | [[Category: Gruetter C]] |
| - | [[Category: Rauh, D]] | + | [[Category: Rauh D]] |
| - | [[Category: Alanine gatekeeper]]
| + | |
| - | [[Category: Cfg]]
| + | |
| - | [[Category: Protein kinase]]
| + | |
| - | [[Category: Pseudo kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase brassinosteroid-signaling]]
| + | |
| Structural highlights
Function
BSK8_ARATH Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Functions redundantly with BSK3, BSK4, BSK6 and BSK7 (PubMed:23496207). Involved in the regulation of sucrose-phosphate synthase 1 (SPS1) in the context of sucrose resuply after starvation. Activates BSL2, a phosphatase that may dephosphorylate SPS1, leading to the activation of SPS1 (PubMed:24924143).[1] [2]
Publication Abstract from PubMed
Brassinosteroid signaling kinases (BSKs) are plant-specific receptor-like cytoplasmic protein kinases involved in the brassinosteroid signaling pathway. Unlike common protein kinases, they possess a naturally occurring alanine residue at the "gatekeeper" position, as well as other sequence variations. How BSKs activate downstream proteins such as BSU1, as well as the structural consequences of their unusual sequential features, was unclear. We crystallized the catalytic domain of BSK8 and solved its structure by multiple-wavelength anomalous dispersion phasing methods to a resolution of 1.5A. In addition, a co-crystal structure of BSK8 with 5-adenylyl imidodiphosphate (AMP-PNP) revealed unusual conformational arrangements of the nucleotide phosphate groups and catalytic key motifs, typically not observed for active protein kinases. Sequential analysis and comparisons with known pseudokinase structures suggest that BSKs represent constitutively inactive protein kinases that regulate brassinosteroid signal transfer through an allosteric mechanism.
Structural Characterization of the RLCK Family Member BSK8: A Pseudokinase with an Unprecedented Architecture.,Grutter C, Sreeramulu S, Sessa G, Rauh D J Mol Biol. 2013 Aug 2. pii: S0022-2836(13)00482-8. doi:, 10.1016/j.jmb.2013.07.034. PMID:23911552[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sreeramulu S, Mostizky Y, Sunitha S, Shani E, Nahum H, Salomon D, Hayun LB, Gruetter C, Rauh D, Ori N, Sessa G. BSKs are partially redundant positive regulators of brassinosteroid signaling in Arabidopsis. Plant J. 2013 Jun;74(6):905-19. doi: 10.1111/tpj.12175. Epub 2013 Apr 15. PMID:23496207 doi:http://dx.doi.org/10.1111/tpj.12175
- ↑ Wu X, Sklodowski K, Encke B, Schulze WX. A kinase-phosphatase signaling module with BSK8 and BSL2 involved in regulation of sucrose-phosphate synthase. J Proteome Res. 2014 Jul 3;13(7):3397-409. doi: 10.1021/pr5003164. Epub 2014 Jun , 20. PMID:24924143 doi:http://dx.doi.org/10.1021/pr5003164
- ↑ Grutter C, Sreeramulu S, Sessa G, Rauh D. Structural Characterization of the RLCK Family Member BSK8: A Pseudokinase with an Unprecedented Architecture. J Mol Biol. 2013 Aug 2. pii: S0022-2836(13)00482-8. doi:, 10.1016/j.jmb.2013.07.034. PMID:23911552 doi:10.1016/j.jmb.2013.07.034
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