3cvr
From Proteopedia
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- | [[Image:3cvr.png|left|200px]] | ||
- | + | ==Crystal structure of the full length IpaH3== | |
+ | <StructureSection load='3cvr' size='340' side='right'caption='[[3cvr]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3cvr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri_2a_str._301 Shigella flexneri 2a str. 301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CVR FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=3cvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cvr OCA], [https://pdbe.org/3cvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cvr RCSB], [https://www.ebi.ac.uk/pdbsum/3cvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cvr ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/IPA3_SHIFL IPA3_SHIFL] 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. Synthesizes a 'Lys-48'-linked ubiquitin chain, which requires non-covalent binding between ubiquitin and the host ubiquitin-conjugating enzyme UBE2D1.<ref>PMID:18997779</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cvr_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=3cvr ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bacterial pathogens have evolved effector proteins with ubiquitin E3 ligase activities through structural mimicking. Here we report the crystal structure of the Shigella flexneri type III effector IpaH3, a member of the leucine-rich repeat (LRR)-containing bacterial E3 family. The LRR domain is structurally similar to Yersinia pestis YopM and potentially binds to substrates. The structure of the C-terminal E3 domain differs from the typical RING- and HECT-type E3s. IpaH3 synthesizes a Lys48-linked ubiquitin chain, and the reaction requires noncovalent binding between ubiquitin and a specific E2, UbcH5. Free ubiquitin serves as an acceptor for IpaH3-catalyzed ubiquitin transfer. Cys363 within a conserved CXD motif acts as a nucleophile to catalyze ubiquitin transfer through a transthiolation reaction. The D365N mutant is devoid of E3 activities but turns into a potent ubiquitin-E2 thioesterase. Our analysis establishes a structurally and mechanistically distinct class of ubiquitin ligases found exclusively in pathogenic or symbiotic bacteria. | ||
- | + | Structure of a Shigella effector reveals a new class of ubiquitin ligases.,Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F Nat Struct Mol Biol. 2008 Dec;15(12):1302-8. Epub 2008 Nov 9. PMID:18997779<ref>PMID:18997779</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3cvr" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Shigella flexneri 2a str. 301]] |
- | [[Category: | + | [[Category: Shao F]] |
- | [[Category: | + | [[Category: Zhu Y]] |
- | + |
Current revision
Crystal structure of the full length IpaH3
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