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| | ==Crystal structure of the CG11501 protein in P21212 spacegroup== | | ==Crystal structure of the CG11501 protein in P21212 spacegroup== |
| - | <StructureSection load='3zzr' size='340' side='right' caption='[[3zzr]], [[Resolution|resolution]] 1.45Å' scene=''> | + | <StructureSection load='3zzr' size='340' side='right'caption='[[3zzr]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zzr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZZR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zzr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZZR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 1.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zzo|3zzo]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></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=3zzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zzr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zzr RCSB], [http://www.ebi.ac.uk/pdbsum/3zzr PDBsum]</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=3zzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zzr OCA], [https://pdbe.org/3zzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zzr RCSB], [https://www.ebi.ac.uk/pdbsum/3zzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zzr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DIE_DROME DIE_DROME] Cytokine which promotes survival following infection by Sindbis virus by suppressing the immune deficiency pathway (PubMed:26739560). Following infection by the enteropathogenic bacteria E.carotovora limits intestinal stem cells proliferation (PubMed:30036358). When secreted from muscle or adipose tissue, can attenuate age-related intestinal tissue degeneration by inhibiting apoptosis (PubMed:30036358).<ref>PMID:26739560</ref> <ref>PMID:30036358</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3zzr" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Drosophila melanogaster]] | | [[Category: Drosophila melanogaster]] |
| - | [[Category: Coste, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Roussel, A]] | + | [[Category: Coste F]] |
| - | [[Category: Immune response]] | + | [[Category: Roussel A]] |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
DIE_DROME Cytokine which promotes survival following infection by Sindbis virus by suppressing the immune deficiency pathway (PubMed:26739560). Following infection by the enteropathogenic bacteria E.carotovora limits intestinal stem cells proliferation (PubMed:30036358). When secreted from muscle or adipose tissue, can attenuate age-related intestinal tissue degeneration by inhibiting apoptosis (PubMed:30036358).[1] [2]
Publication Abstract from PubMed
BACKGROUND: The Drosophila melanogaster gene CG11501 is up regulated after a septic injury and was proposed to act as a negative regulator of the JAK/STAT signaling pathway. Diedel, the CG11501 gene product, is a small protein of 115 residues with 10 cysteines. METHODOLOGY/PRINCIPAL FINDINGS: We have produced Diedel in Drosophila S2 cells as an extra cellular protein thanks to its own signal peptide and solved its crystal structure at 1.15 A resolution by SIRAS using an iodo derivative. Diedel is composed of two sub domains SD1 and SD2. SD1 is made of an antiparallel beta-sheet covered by an alpha-helix and displays a ferredoxin-like fold. SD2 reveals a new protein fold made of loops connected by four disulfide bridges. Further structural analysis identified conserved hydrophobic residues on the surface of Diedel that may constitute a potential binding site. The existence of two conformations, cis and trans, for the proline 52 may be of interest as prolyl peptidyl isomerisation has been shown to play a role in several physiological mechanisms. The genome of D. melanogaster contains two other genes coding for proteins homologous to Diedel, namely CG43228 and CG34329. Strikingly, apart from Drosophila and the pea aphid Acyrthosiphon pisum, Diedel-related sequences were exclusively identified in a few insect DNA viruses of the Baculoviridae and Ascoviridae families. CONCLUSION/SIGNIFICANCE: Diedel, a marker of the Drosophila antimicrobial/antiviral response, is a member of a small family of proteins present in drosophilids, aphids and DNA viruses infecting lepidopterans. Diedel is an extracellular protein composed of two sub-domains. Two special structural features (hydrophobic surface patch and cis/trans conformation for proline 52) may indicate a putative interaction site, and support an extra cellular signaling function for Diedel, which is in accordance with its proposed role as negative regulator of the JAK/STAT signaling pathway.
Crystal structure of Diedel, a marker of the immune response of Drosophila melanogaster.,Coste F, Kemp C, Bobezeau V, Hetru C, Kellenberger C, Imler JL, Roussel A PLoS One. 2012;7(3):e33416. Epub 2012 Mar 19. PMID:22442689[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lamiable O, Kellenberger C, Kemp C, Troxler L, Pelte N, Boutros M, Marques JT, Daeffler L, Hoffmann JA, Roussel A, Imler JL. Cytokine Diedel and a viral homologue suppress the IMD pathway in Drosophila. Proc Natl Acad Sci U S A. 2016 Jan 19;113(3):698-703. PMID:26739560 doi:10.1073/pnas.1516122113
- ↑ Mlih M, Khericha M, Birdwell C, West AP, Karpac J. A virus-acquired host cytokine controls systemic aging by antagonizing apoptosis. PLoS Biol. 2018 Jul 23;16(7):e2005796. PMID:30036358 doi:10.1371/journal.pbio.2005796
- ↑ Coste F, Kemp C, Bobezeau V, Hetru C, Kellenberger C, Imler JL, Roussel A. Crystal structure of Diedel, a marker of the immune response of Drosophila melanogaster. PLoS One. 2012;7(3):e33416. Epub 2012 Mar 19. PMID:22442689 doi:10.1371/journal.pone.0033416
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