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| | <StructureSection load='4kqa' size='340' side='right'caption='[[4kqa]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4kqa' size='340' side='right'caption='[[4kqa]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kqa]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KQA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kqa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KQA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kqa OCA], [https://pdbe.org/4kqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kqa RCSB], [https://www.ebi.ac.uk/pdbsum/4kqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kqa ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kqb|4kqb]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CELE_H03A11.1, H03A11.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4kqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kqa OCA], [http://pdbe.org/4kqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kqa RCSB], [http://www.ebi.ac.uk/pdbsum/4kqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kqa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FA20C_CAEEL FA20C_CAEEL] Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs.<ref>PMID:23754375</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xiao, J]] | + | [[Category: Xiao J]] |
| - | [[Category: Secreted kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
FA20C_CAEEL Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs.[1]
Publication Abstract from PubMed
The family with sequence similarity 20 (Fam20) kinases phosphorylate extracellular substrates and play important roles in biomineralization. Fam20C is the Golgi casein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Mutations in Fam20C cause Raine syndrome, an osteosclerotic bone dysplasia. Here we report the crystal structure of the Fam20C ortholog from Caenorhabditis elegans. The nucleotide-free and Mn/ADP-bound structures unveil an atypical protein kinase-like fold and highlight residues critical for activity. The position of the regulatory alphaC helix and the lack of an activation loop indicate an architecture primed for efficient catalysis. Furthermore, several distinct elements, including the presence of disulfide bonds, suggest that the Fam20 family diverged early in the evolution of the protein kinase superfamily. Our results reinforce the structural diversity of protein kinases and have important implications for patients with disorders of biomineralization.
Crystal structure of the Golgi casein kinase.,Xiao J, Tagliabracci VS, Wen J, Kim SA, Dixon JE Proc Natl Acad Sci U S A. 2013 Jun 10. PMID:23754375[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xiao J, Tagliabracci VS, Wen J, Kim SA, Dixon JE. Crystal structure of the Golgi casein kinase. Proc Natl Acad Sci U S A. 2013 Jun 10. PMID:23754375 doi:10.1073/pnas.1309211110
- ↑ Xiao J, Tagliabracci VS, Wen J, Kim SA, Dixon JE. Crystal structure of the Golgi casein kinase. Proc Natl Acad Sci U S A. 2013 Jun 10. PMID:23754375 doi:10.1073/pnas.1309211110
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