2qyu
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='2qyu' size='340' side='right'caption='[[2qyu]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2qyu' size='340' side='right'caption='[[2qyu]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2qyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2qyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._SL1344 Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QYU FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=2qyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qyu OCA], [https://pdbe.org/2qyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qyu RCSB], [https://www.ebi.ac.uk/pdbsum/2qyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qyu 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=2qyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qyu OCA], [https://pdbe.org/2qyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qyu RCSB], [https://www.ebi.ac.uk/pdbsum/2qyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qyu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/SOPA_SALTY SOPA_SALTY] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.<ref>PMID:17076670</ref> <ref>PMID:18066077</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 21: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qyu ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qyu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Bacterial pathogens deliver virulence proteins into host cells to facilitate entry and survival. Salmonella SopA functions as an E3 ligase to manipulate the host proinflammatory response. Here we report the crystal structure of SopA in two conformations. Although it has little sequence similarity to eukaryotic HECT-domain E3s, the C-terminal half of SopA has a bilobal architecture that is reminiscent of the N- and C-lobe arrangement of HECT domains. The SopA structure also contains a putative substrate-binding domain located near the E2-binding site. The two structures of SopA differ in the relative orientations of the C lobe, indicating that SopA possesses the conformational flexibility essential for HECT E3 function. These results suggest that SopA is a unique HECT E3 ligase evolved from the coevolutionary selective pressure at the bacterium-host interface. | ||
- | |||
- | Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase.,Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J Nat Struct Mol Biol. 2008 Jan;15(1):65-70. Epub 2007 Dec 9. PMID:18066077<ref>PMID:18066077</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2qyu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Line 38: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]] |
- | [[Category: Chen | + | [[Category: Chen J]] |
- | [[Category: Diao | + | [[Category: Diao J]] |
- | + | ||
- | + |
Current revision
Crystal structure of Salmonella effector protein SopA
|