3l3p

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<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=3l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l3p RCSB], [http://www.ebi.ac.uk/pdbsum/3l3p 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=3l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l3p RCSB], [http://www.ebi.ac.uk/pdbsum/3l3p PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/IPA9_SHIFL IPA9_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 and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell. Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), an ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG. Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection. Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme.<ref>PMID:15950937</ref> <ref>PMID:18005683</ref> <ref>PMID:20010814</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 15:49, 25 December 2014

Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap

3l3p, resolution 3.20Å

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