3ckd
From Proteopedia
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- | [[Image:3ckd.png|left|200px]] | ||
- | + | ==Crystal structure of the C-terminal domain of the Shigella type III effector IpaH== | |
+ | <StructureSection load='3ckd' size='340' side='right'caption='[[3ckd]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3ckd]] is a 3 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=3CKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CKD 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]] 2.65Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3ckd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ckd OCA], [https://pdbe.org/3ckd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ckd RCSB], [https://www.ebi.ac.uk/pdbsum/3ckd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ckd ProSAT], [https://www.topsan.org/Proteins/MCSG/3ckd TOPSAN]</span></td></tr> | ||
+ | </table> | ||
+ | == 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/ck/3ckd_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=3ckd ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | IpaH proteins are E3 ubiquitin ligases delivered by the type III secretion apparatus into host cells upon infection of humans by the Gram-negative pathogen Shigella flexneri. These proteins comprise a variable leucine-rich repeat-containing N-terminal domain and a conserved C-terminal domain harboring an invariant cysteine residue that is crucial for activity. IpaH homologs are encoded by diverse animal and plant pathogens. Here we demonstrate that the IpaH C-terminal domain carries the catalytic activity for ubiquitin transfer and that the N-terminal domain carries the substrate specificity. The structure of the IpaH C-terminal domain, determined to 2.65-A resolution, represents an all-helical fold bearing no resemblance to previously defined E3 ubiquitin ligases. The conserved and essential cysteine residue lies on a flexible, surface-exposed loop surrounded by conserved acidic residues, two of which are crucial for IpaH activity. | ||
- | + | Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases.,Singer AU, Rohde JR, Lam R, Skarina T, Kagan O, Dileo R, Chirgadze NY, Cuff ME, Joachimiak A, Tyers M, Sansonetti PJ, Parsot C, Savchenko A Nat Struct Mol Biol. 2008 Dec;15(12):1293-301. Epub 2008 Nov 9. PMID:18997778<ref>PMID:18997778</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3ckd" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
[[Category: Shigella flexneri 2a str. 301]] | [[Category: Shigella flexneri 2a str. 301]] | ||
- | + | [[Category: Cuff ME]] | |
- | [[Category: Cuff | + | [[Category: DiLeo R]] |
- | [[Category: DiLeo | + | [[Category: Edwards AM]] |
- | [[Category: Edwards | + | [[Category: Joachimiak A]] |
- | [[Category: Joachimiak | + | [[Category: Kagan O]] |
- | [[Category: Kagan | + | [[Category: Lam R]] |
- | [[Category: Lam | + | [[Category: Savchenko A]] |
- | + | [[Category: Singer AU]] | |
- | [[Category: Savchenko | + | [[Category: Skarina T]] |
- | [[Category: Singer | + | |
- | [[Category: Skarina | + | |
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Current revision
Crystal structure of the C-terminal domain of the Shigella type III effector IpaH
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