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| | ==Structure of the BSK8 kinase domain (SeMet labeled)== | | ==Structure of the BSK8 kinase domain (SeMet labeled)== |
| - | <StructureSection load='4i93' size='340' side='right' caption='[[4i93]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='4i93' size='340' side='right'caption='[[4i93]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i93]] is a 2 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=4I93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I93 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i93]] is a 2 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=4I93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I93 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i92|4i92]], [[4i94|4i94]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i93 OCA], [https://pdbe.org/4i93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i93 RCSB], [https://www.ebi.ac.uk/pdbsum/4i93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i93 ProSAT]</span></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=4i93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i93 OCA], [http://pdbe.org/4i93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i93 RCSB], [http://www.ebi.ac.uk/pdbsum/4i93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i93 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4i93" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4i93" 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: Semet derivative]]
| + | |
| - | [[Category: Transferase]]
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| - | [[Category: Transferase brassinosteroid-signaling]]
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| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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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