7v8h

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of LRR domain from Shigella flexneri IpaH1.4

Structural highlights

7v8h is a 2 chain structure with sequence from Shigella flexneri 5a str. M90T. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.46Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IPA14_SHIFL E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP (PubMed:27572974). Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria (PubMed:27572974). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:27572974, PubMed:28481331). By promoting degradation of host RNF31/HOIP, IpaH1.4 prevents formation of the bacterial ubiquitin coat and activation of host cell innate immunity (PubMed:27572974, PubMed:28481331).^[1] ^[2]

Publication Abstract from PubMed

SignificanceShigella flexneri, a deleterious bacterium, causes massive human infection cases and deaths worldwide. To facilitate survival and replication in infected host cells, S. flexneri can secrete two highly similar E3 ligase effectors, IpaH1.4 and IpaH2.5, to subvert the linear ubiquitin chain assembly complex (LUBAC), a key player involved in numerous antibacterial signaling pathways of host cells but with poorly understood mechanisms. In this study, through systematic biochemical and structural characterization, we elucidate the multiple tactics adopted by IpaH1.4/2.5 to disarm the human LUBAC and provide mechanistic insights into the subversion of host LUBAC by IpaH1.4/2.5 of S. flexneri.

Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri.,Liu J, Wang Y, Wang D, Wang Y, Xu X, Zhang Y, Li Y, Zhang M, Gong X, Tang Y, Shen L, Li M, Pan L Proc Natl Acad Sci U S A. 2022 Mar 22;119(12):e2116776119. doi:, 10.1073/pnas.2116776119. Epub 2022 Mar 16. PMID:35294289^[3]

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

References

↑ de Jong MF, Liu Z, Chen D, Alto NM. Shigella flexneri suppresses NF-κB activation by inhibiting linear ubiquitin chain ligation. Nat Microbiol. 2016 May 27;1(7):16084. PMID:27572974 doi:10.1038/nmicrobiol.2016.84
↑ Noad J, von der Malsburg A, Pathe C, Michel MA, Komander D, Randow F. LUBAC-synthesized linear ubiquitin chains restrict cytosol-invading bacteria by activating autophagy and NF-κB. Nat Microbiol. 2017 May 8;2:17063. PMID:28481331 doi:10.1038/nmicrobiol.2017.63
↑ Liu J, Wang Y, Wang D, Wang Y, Xu X, Zhang Y, Li Y, Zhang M, Gong X, Tang Y, Shen L, Li M, Pan L. Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri. Proc Natl Acad Sci U S A. 2022 Mar 22;119(12):e2116776119. PMID:35294289 doi:10.1073/pnas.2116776119

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7v8h"

Categories: Large Structures | Shigella flexneri 5a str. M90T | Liu J | Pan L | Wang Y

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7v8h is ON HOLD  until Paper Publication
+==Crystal structure of LRR domain from Shigella flexneri IpaH1.4==
+<StructureSection load='7v8h' size='340' side='right'caption='[[7v8h]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7v8h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri_5a_str._M90T Shigella flexneri 5a str. M90T]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V8H 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]] 2.46&#8491;</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=7v8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v8h OCA], [https://pdbe.org/7v8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v8h RCSB], [https://www.ebi.ac.uk/pdbsum/7v8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v8h ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IPA14_SHIFL IPA14_SHIFL] E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP (PubMed:27572974). Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria (PubMed:27572974). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:27572974, PubMed:28481331). By promoting degradation of host RNF31/HOIP, IpaH1.4 prevents formation of the bacterial ubiquitin coat and activation of host cell innate immunity (PubMed:27572974, PubMed:28481331).<ref>PMID:27572974</ref> <ref>PMID:28481331</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+SignificanceShigella flexneri, a deleterious bacterium, causes massive human infection cases and deaths worldwide. To facilitate survival and replication in infected host cells, S. flexneri can secrete two highly similar E3 ligase effectors, IpaH1.4 and IpaH2.5, to subvert the linear ubiquitin chain assembly complex (LUBAC), a key player involved in numerous antibacterial signaling pathways of host cells but with poorly understood mechanisms. In this study, through systematic biochemical and structural characterization, we elucidate the multiple tactics adopted by IpaH1.4/2.5 to disarm the human LUBAC and provide mechanistic insights into the subversion of host LUBAC by IpaH1.4/2.5 of S. flexneri.
-Authors:
+Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri.,Liu J, Wang Y, Wang D, Wang Y, Xu X, Zhang Y, Li Y, Zhang M, Gong X, Tang Y, Shen L, Li M, Pan L Proc Natl Acad Sci U S A. 2022 Mar 22;119(12):e2116776119. doi:, 10.1073/pnas.2116776119. Epub 2022 Mar 16. PMID:35294289<ref>PMID:35294289</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7v8h" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Shigella flexneri 5a str. M90T]]
+[[Category: Liu J]]
+[[Category: Pan L]]
+[[Category: Wang Y]]

7v8h

From Proteopedia

Current revision

Crystal structure of LRR domain from Shigella flexneri IpaH1.4

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox