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| | <StructureSection load='2jd5' size='340' side='right'caption='[[2jd5]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2jd5' size='340' side='right'caption='[[2jd5]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jd5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JD5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JD5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jd5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JD5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1how|1how]], [[1q8y|1q8y]], [[1q8z|1q8z]], [[1q97|1q97]], [[1q99|1q99]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2jd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jd5 OCA], [https://pdbe.org/2jd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jd5 RCSB], [https://www.ebi.ac.uk/pdbsum/2jd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jd5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jd5 OCA], [http://pdbe.org/2jd5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jd5 RCSB], [http://www.ebi.ac.uk/pdbsum/2jd5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jd5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SKY1_YEAST SKY1_YEAST]] Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.<ref>PMID:11175909</ref> [[http://www.uniprot.org/uniprot/NOP3_YEAST NOP3_YEAST]] Required for pre-rRNA processing and nuclear import as well as mitochondrial protein targeting. Binds to poly(A). | + | [https://www.uniprot.org/uniprot/SKY1_YEAST SKY1_YEAST] Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.<ref>PMID:11175909</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Adams, J A]] | + | [[Category: Adams JA]] |
| - | [[Category: Ghosh, G]] | + | [[Category: Ghosh G]] |
| - | [[Category: Huang, D]] | + | [[Category: Huang D]] |
| - | [[Category: Lukasiewicz, R]] | + | [[Category: Lukasiewicz R]] |
| - | [[Category: Nolen, B]] | + | [[Category: Nolen B]] |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Mrna export protein]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Serine/threonine-protein kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SKY1_YEAST Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.[1]
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
The SR protein kinase in yeast, Sky1p, phosphorylates yeast SR-like protein, Npl3p, at a single serine residue located at its C terminus. We report here the X-ray crystal structure of Sky1p bound to a substrate peptide and ADP. Surprisingly, an Npl3p-derived substrate peptide occupies a groove 20 A away from the kinase active site. In vitro studies support the substrate-docking role of this groove. Mutagenesis and binding studies reveal that multiple degenerate short peptide motifs located within the RGG domain of Npl3p serve as the substrate docking motifs. However, a single docking motif is sufficient for its stable interaction with the kinase. Methylation of the docking motifs abolishes kinase binding and phosphorylation of Npl3p. Remarkably, removal of the docking groove in the kinase or the docking motifs of the substrate does not reduce the overall catalytic efficiency of the phosphorylation reaction in any significant manner. We suggest that docking interaction between Sky1p and Npl3p is essential for substrate recruitment and binding specificity.
The RGG domain of Npl3p recruits Sky1p through docking interactions.,Lukasiewicz R, Nolen B, Adams JA, Ghosh G J Mol Biol. 2007 Mar 16;367(1):249-61. Epub 2006 Dec 19. PMID:17239901[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, Ghosh G. The structure of Sky1p reveals a novel mechanism for constitutive activity. Nat Struct Biol. 2001 Feb;8(2):176-83. PMID:11175909 doi:10.1038/84178
- ↑ Lukasiewicz R, Nolen B, Adams JA, Ghosh G. The RGG domain of Npl3p recruits Sky1p through docking interactions. J Mol Biol. 2007 Mar 16;367(1):249-61. Epub 2006 Dec 19. PMID:17239901 doi:10.1016/j.jmb.2006.12.031
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