4nkh

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==Crystal structure of SspH1 LRR domain==
==Crystal structure of SspH1 LRR domain==
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<StructureSection load='4nkh' size='340' side='right' caption='[[4nkh]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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<StructureSection load='4nkh' size='340' side='right'caption='[[4nkh]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nkh]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Salt1 Salt1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NKH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nkh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._14028S Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NKH FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nkg|4nkg]]</td></tr>
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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]] 2.75&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sspH1, STM14_1483 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=588858 SALT1])</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=4nkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkh OCA], [https://pdbe.org/4nkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nkh RCSB], [https://www.ebi.ac.uk/pdbsum/4nkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nkh ProSAT]</span></td></tr>
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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=4nkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nkh RCSB], [http://www.ebi.ac.uk/pdbsum/4nkh PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SSPH1_SALT1 SSPH1_SALT1] 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. Can ubiquitinate both ubiquitin and host PKN1. Down-modulates production of host proinflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression, probably via interaction with PKN1.<ref>PMID:10564523</ref> <ref>PMID:12819095</ref> <ref>PMID:16611232</ref> <ref>PMID:18005683</ref>
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IpaH proteins are bacterial-specific E3 enzymes that function as T3SS effectors in Salmonella, Shigella, and other gram-negative bacteria. IpaH enzymes recruit host substrates for ubiquitination via an LRR domain, which can inhibit the catalytic domain in the absence of substrate. The basis for substrate recognition and the alleviation of autoinhibition upon substrate binding is unknown. Here we report the X-ray structure of Salmonella SspH1 in complex with human PKN1. The LRR domain of SspH1 interacts specifically with the HR1b coiled-coil sub-domain of PKN1 in manner that sterically displaces the catalytic domain from the LRR domain, and thereby activates catalytic function. SspH1 catalyzes the ubiquitination and proteasome-dependent degradation of PKN1 in cells, which attenuates androgen receptor responsiveness but not NF-kappaB activity. These regulatory features are conserved in other IpaH-substrate interactions. Our results explain the mechanism whereby substrate recognition and enzyme autoregulation are coupled in this class of bacterial effector proteins.
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Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase.,Keszei AF, Tang X, McCormick C, Zeqiraj E, Rohde JR, Tyers M, Sicheri F Mol Cell Biol. 2013 Nov 18. PMID:24248594<ref>PMID:24248594</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Salt1]]
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[[Category: Large Structures]]
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[[Category: Keszei, A F.A]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]]
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[[Category: Mccormick, C]]
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[[Category: Keszei AFA]]
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[[Category: Rohde, J R]]
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[[Category: Mccormick C]]
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[[Category: Sicheri, F]]
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[[Category: Rohde JR]]
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[[Category: Tyers, M]]
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[[Category: Sicheri F]]
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[[Category: Xiaojing, T]]
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[[Category: Tyers M]]
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[[Category: Zeqiraj, E]]
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[[Category: Xiaojing T]]
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[[Category: E3 ligase substrate interaction domain]]
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[[Category: Zeqiraj E]]
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[[Category: Leucine-rich repeat]]
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[[Category: Ligase]]
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Current revision

Crystal structure of SspH1 LRR domain

PDB ID 4nkh

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