5f87
From Proteopedia
(Difference between revisions)
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<StructureSection load='5f87' size='340' side='right' caption='[[5f87]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='5f87' size='340' side='right' caption='[[5f87]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5f87]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F87 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f87]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F87 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f85|5f85]], [[5f86|5f86]], [[5f84|5f84]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f85|5f85]], [[5f86|5f86]], [[5f84|5f84]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rumi, CG31152 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=5f87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f87 OCA], [http://pdbe.org/5f87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f87 RCSB], [http://www.ebi.ac.uk/pdbsum/5f87 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f87 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=5f87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f87 OCA], [http://pdbe.org/5f87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f87 RCSB], [http://www.ebi.ac.uk/pdbsum/5f87 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f87 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RUMI_DROME RUMI_DROME]] Protein O-glucosyltransferase. Catalyzes the reaction that attaches glucose through an O-glycosidic linkage to a conserved serine residue in epidermal growth factor-like repeats. Regulates Notch signaling by glucosylating Notch in the ER, glucosylation is required for the correct folding and cleavage of Notch.<ref>PMID:18243100</ref> | [[http://www.uniprot.org/uniprot/RUMI_DROME RUMI_DROME]] Protein O-glucosyltransferase. Catalyzes the reaction that attaches glucose through an O-glycosidic linkage to a conserved serine residue in epidermal growth factor-like repeats. Regulates Notch signaling by glucosylating Notch in the ER, glucosylation is required for the correct folding and cleavage of Notch.<ref>PMID:18243100</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rumi O-glucosylates the EGF repeats of a growing list of proteins essential in metazoan development, including Notch. Rumi is essential for Notch signaling, and Rumi dysregulation is linked to several human diseases. Despite Rumi's critical roles, it is unknown how Rumi glucosylates a serine of many but not all EGF repeats. Here we report crystal structures of Drosophila Rumi as binary and ternary complexes with a folded EGF repeat and/or donor substrates. These structures provide insights into the catalytic mechanism and show that Rumi recognizes structural signatures of the EGF motif, the U-shaped consensus sequence, C-X-S-X-(P/A)-C and a conserved hydrophobic region. We found that five Rumi mutations identified in cancers and Dowling-Degos disease are clustered around the enzyme active site and adversely affect its activity. Our study suggests that loss of Rumi activity may underlie these diseases, and the mechanistic insights may facilitate the development of modulators of Notch signaling. | ||
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| + | Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations.,Yu H, Takeuchi H, Takeuchi M, Liu Q, Kantharia J, Haltiwanger RS, Li H Nat Chem Biol. 2016 Sep;12(9):735-40. doi: 10.1038/nchembio.2135. Epub 2016 Jul, 18. PMID:27428513<ref>PMID:27428513</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5f87" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Drome]] | ||
[[Category: Li, H L]] | [[Category: Li, H L]] | ||
[[Category: Yu, H J]] | [[Category: Yu, H J]] | ||
Revision as of 06:21, 18 April 2018
Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP
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