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3cvr

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Revision as of 13:11, 7 November 2018

Crystal structure of the full length IpaH3

Structural highlights

3cvr is a 1 chain structure with sequence from Shigella flexneri 2a str. 301. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	ipaH_3 (Shigella flexneri 2a str. 301)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

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

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. Structure of a Shigella effector reveals a new class of ubiquitin ligases. Nat Struct Mol Biol. 2008 Dec;15(12):1302-8. Epub 2008 Nov 9. PMID:18997779 doi:10.1038/nsmb.1517
↑ Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. Structure of a Shigella effector reveals a new class of ubiquitin ligases. Nat Struct Mol Biol. 2008 Dec;15(12):1302-8. Epub 2008 Nov 9. PMID:18997779 doi:10.1038/nsmb.1517

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cvr"

Categories: Shigella flexneri 2a str. 301 | Shao, F | Zhu, Y | Leucine rich repeat and alpha fold | Ligase

@@ Line 1: / Line 1: @@
 ==Crystal structure of the full length IpaH3==
 <StructureSection load='3cvr' size='340' side='right' caption='[[3cvr]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ipaH_3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198214 Shigella flexneri 2a str. 301])</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=3cvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cvr OCA], [http://pdbe.org/3cvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cvr RCSB], [http://www.ebi.ac.uk/pdbsum/3cvr PDBsum]</span></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=3cvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cvr OCA], [http://pdbe.org/3cvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cvr RCSB], [http://www.ebi.ac.uk/pdbsum/3cvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cvr ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cvr_consurf.spt"</scriptWhenChecked>
+    <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/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3cvr

From Proteopedia

Revision as of 13:11, 7 November 2018

Crystal structure of the full length IpaH3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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