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| | ==Dimerization domain of Vibrio parahemolyticus VopL== | | ==Dimerization domain of Vibrio parahemolyticus VopL== |
| - | <StructureSection load='3ryl' size='340' side='right' caption='[[3ryl]], [[Resolution|resolution]] 3.10Å' scene=''> | + | <StructureSection load='3ryl' size='340' side='right'caption='[[3ryl]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ryl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibpa Vibpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RYL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ryl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus_RIMD_2210633 Vibrio parahaemolyticus RIMD 2210633]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RYL FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VopL, VPA1370 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223926 VIBPA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ryl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ryl OCA], [http://pdbe.org/3ryl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ryl RCSB], [http://www.ebi.ac.uk/pdbsum/3ryl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ryl 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=3ryl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ryl OCA], [https://pdbe.org/3ryl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ryl RCSB], [https://www.ebi.ac.uk/pdbsum/3ryl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ryl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q87GE5_VIBPA Q87GE5_VIBPA] |
| | <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: Vibpa]] | + | [[Category: Large Structures]] |
| - | [[Category: Dominguez, R]] | + | [[Category: Vibrio parahaemolyticus RIMD 2210633]] |
| - | [[Category: Namgoong, S]] | + | [[Category: Dominguez R]] |
| - | [[Category: Actin nucleation]] | + | [[Category: Namgoong S]] |
| - | [[Category: Filament pointed end binding]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
Q87GE5_VIBPA
Publication Abstract from PubMed
Pathogen proteins targeting the actin cytoskeleton often serve as model systems to understand their more complex eukaryotic analogs. We show that the strong actin filament nucleation activity of Vibrio parahaemolyticus VopL depends on its three W domains and on its dimerization through a unique VopL C-terminal domain (VCD). The VCD shows a previously unknown all-helical fold and interacts with the pointed end of the actin nucleus, contributing to the nucleation activity directly and through duplication of the W domain repeat. VopL promotes rapid cycles of filament nucleation and detachment but generally has no effect on elongation. Profilin inhibits VopL-induced nucleation by competing for actin binding to the W domains. Combined, the results suggest that VopL stabilizes a hexameric double-stranded pointed end nucleus. Analysis of hybrid constructs of VopL and the eukaryotic nucleator Spire suggest that Spire may also function as a dimer in cells.
Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation.,Namgoong S, Boczkowska M, Glista MJ, Winkelman JD, Rebowski G, Kovar DR, Dominguez R Nat Struct Mol Biol. 2011 Aug 28;18(9):1060-7. doi: 10.1038/nsmb.2109. PMID:21873985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Namgoong S, Boczkowska M, Glista MJ, Winkelman JD, Rebowski G, Kovar DR, Dominguez R. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nat Struct Mol Biol. 2011 Aug 28;18(9):1060-7. doi: 10.1038/nsmb.2109. PMID:21873985 doi:10.1038/nsmb.2109
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