3l3p

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{{STRUCTURE_3l3p| PDB=3l3p | SCENE= }}
 
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===Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap===
 
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{{ABSTRACT_PUBMED_20831869}}
 
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==Function==
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==Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap==
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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>
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<StructureSection load='3l3p' size='340' side='right'caption='[[3l3p]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3l3p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L3P FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3p OCA], [https://pdbe.org/3l3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l3p RCSB], [https://www.ebi.ac.uk/pdbsum/3l3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/3l3p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3l3p ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We show that the monomeric form of Shigella IpaH9.8 E3 ligase catalyses the ubiquitination of human U2AF35 in vitro, providing a molecular mechanism for the observed in vivo effect. We further discover that under non-reducing conditions IpaH9.8 undergoes a domain swap driven by the formation of a disulfide bridge involving the catalytic cysteine and that this dimer is unable to catalyse the ubiquitination of U2AF35. The crystal structure of the domain-swapped dimer is presented. The redox inactivation of IpaH9.8 could be a mechanism of regulating the activity of the IpaH9.8 E3 ligase in response to cell damage so that the host cell in which the bacteria resides is maintained in a benign state suitable for bacterial survival.
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==About this Structure==
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A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase.,Seyedarabi A, Sullivan JA, Sasakawa C, Pickersgill RW FEBS Lett. 2010 Oct 8;584(19):4163-8. Epub 2010 Sep 8. PMID:20831869<ref>PMID:20831869</ref>
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[[3l3p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L3P OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:020831869</ref><references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 3l3p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Shigella flexneri]]
[[Category: Shigella flexneri]]
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[[Category: Ubiquitin--protein ligase]]
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[[Category: Pickersgill RW]]
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[[Category: Pickersgill, R W.]]
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[[Category: Sasakawa C]]
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[[Category: Sasakawa, C.]]
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[[Category: Seyedarabi A]]
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[[Category: Seyedarabi, A.]]
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[[Category: Sullivan JA]]
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[[Category: Sullivan, J A.]]
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[[Category: Cxd motif]]
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[[Category: Domain swap]]
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[[Category: E3 ligase]]
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[[Category: Ligase]]
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Current revision

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

PDB ID 3l3p

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