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| | <StructureSection load='2ihs' size='340' side='right'caption='[[2ihs]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2ihs' size='340' side='right'caption='[[2ihs]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ihs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ihs]] is a 4 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=2IHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHS FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fnj|2fnj]], [[2fbe|2fbe]]</div></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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gus ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2ihs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihs OCA], [https://pdbe.org/2ihs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ihs RCSB], [https://www.ebi.ac.uk/pdbsum/2ihs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihs ProSAT]</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=2ihs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihs OCA], [https://pdbe.org/2ihs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ihs RCSB], [https://www.ebi.ac.uk/pdbsum/2ihs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/VASA1_DROME VASA1_DROME]] Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles during germ cell formation. Required for gus, Fsn and aub accumulation at the posterior pole of the embryo. Required for the localization of vas to the perinuclear region of nurse cells.<ref>PMID:10678180</ref> <ref>PMID:11526087</ref> <ref>PMID:12479811</ref> <ref>PMID:14588248</ref> <ref>PMID:16630817</ref> <ref>PMID:18590813</ref> <ref>PMID:20123973</ref> <ref>PMID:3052853</ref> <ref>PMID:3140040</ref> <ref>PMID:8026330</ref> <ref>PMID:9521895</ref>
| + | [https://www.uniprot.org/uniprot/GUS_DROME GUS_DROME] Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.<ref>PMID:12479811</ref> <ref>PMID:20123973</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: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oh, B H]] | + | [[Category: Oh BH]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park SY]] |
| - | [[Category: Woo, J S]] | + | [[Category: Woo JS]] |
| - | [[Category: B30 2/spry]]
| + | |
| - | [[Category: F-box-spry]]
| + | |
| - | [[Category: Gustavus]]
| + | |
| - | [[Category: Peptide binding protein]]
| + | |
| - | [[Category: Spry-containing socs box]]
| + | |
| - | [[Category: Trim family]]
| + | |
| - | [[Category: Vasa]]
| + | |
| Structural highlights
Function
GUS_DROME Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.[1] [2]
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
B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.
Structural basis for protein recognition by B30.2/SPRY domains.,Woo JS, Suh HY, Park SY, Oh BH Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Styhler S, Nakamura A, Lasko P. VASA localization requires the SPRY-domain and SOCS-box containing protein, GUSTAVUS. Dev Cell. 2002 Dec;3(6):865-76. PMID:12479811
- ↑ Kugler JM, Woo JS, Oh BH, Lasko P. Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors. Mol Cell Biol. 2010 Apr;30(7):1769-82. doi: 10.1128/MCB.01100-09. Epub 2010 Feb, 1. PMID:20123973 doi:http://dx.doi.org/10.1128/MCB.01100-09
- ↑ Woo JS, Suh HY, Park SY, Oh BH. Structural basis for protein recognition by B30.2/SPRY domains. Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197 doi:10.1016/j.molcel.2006.11.009
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