5b0n: Difference between revisions

Revision as of 06:33, 31 May 2023

Structure of Shigella effector LRR domain

Structural highlights

5b0n is a 2 chain structure with sequence from Shigella flexneri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Infectious diseases caused by bacteria have significant impacts on global public health. During infection, pathogenic bacteria deliver a variety of virulence factors, called effectors, into host cells. The Shigella effector IpaH9.8 functions as an ubiquitin ligase, ubiquitinating the NF-kappaB essential modulator (NEMO)/IKK-gamma to inhibit host inflammatory responses. IpaH9.8 contains leucine-rich repeats (LRRs) involved in substrate recognition and an E3 ligase domain. To elucidate the structural basis of the function of IpaH9.8, the crystal structure of the LRR domain of Shigella IpaH9.8 was determined and this structure was compared with the known structures of other IpaH family members. This model provides insights into the structural features involved in substrate specificity.

Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8.,Takagi K, Kim M, Sasakawa C, Mizushima T Acta Crystallogr F Struct Biol Commun. 2016 Apr 1;72(Pt 4):269-75. doi:, 10.1107/S2053230X16002715. Epub 2016 Mar 16. PMID:27050259^[4]

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

References

↑ Okuda J, Toyotome T, Kataoka N, Ohno M, Abe H, Shimura Y, Seyedarabi A, Pickersgill R, Sasakawa C. Shigella effector IpaH9.8 binds to a splicing factor U2AF(35) to modulate host immune responses. Biochem Biophys Res Commun. 2005 Jul 29;333(2):531-9. PMID:15950937 doi:10.1016/j.bbrc.2005.05.145
↑ Rohde JR, Breitkreutz A, Chenal A, Sansonetti PJ, Parsot C. Type III secretion effectors of the IpaH family are E3 ubiquitin ligases. Cell Host Microbe. 2007 Mar 15;1(1):77-83. PMID:18005683 doi:10.1016/j.chom.2007.02.002
↑ Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol. 2010 Jan;12(1):66-73; sup pp 1-9. doi: 10.1038/ncb2006. Epub 2009 , Dec 13. PMID:20010814 doi:10.1038/ncb2006
↑ Takagi K, Kim M, Sasakawa C, Mizushima T. Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8. Acta Crystallogr F Struct Biol Commun. 2016 Apr 1;72(Pt 4):269-75. doi:, 10.1107/S2053230X16002715. Epub 2016 Mar 16. PMID:27050259 doi:https://dx.doi.org/10.1107/S2053230X16002715

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Okuda J, Toyotome T, Kataoka N, Ohno M, Abe H, Shimura Y, Seyedarabi A, Pickersgill R, Sasakawa C. Shigella effector IpaH9.8 binds to a splicing factor U2AF(35) to modulate host immune responses. Biochem Biophys Res Commun. 2005 Jul 29;333(2):531-9. PMID:15950937 doi:10.1016/j.bbrc.2005.05.145

[2] Rohde JR, Breitkreutz A, Chenal A, Sansonetti PJ, Parsot C. Type III secretion effectors of the IpaH family are E3 ubiquitin ligases. Cell Host Microbe. 2007 Mar 15;1(1):77-83. PMID:18005683 doi:10.1016/j.chom.2007.02.002

[3] Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol. 2010 Jan;12(1):66-73; sup pp 1-9. doi: 10.1038/ncb2006. Epub 2009 , Dec 13. PMID:20010814 doi:10.1038/ncb2006

[4] Takagi K, Kim M, Sasakawa C, Mizushima T. Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8. Acta Crystallogr F Struct Biol Commun. 2016 Apr 1;72(Pt 4):269-75. doi:, 10.1107/S2053230X16002715. Epub 2016 Mar 16. PMID:27050259 doi:https://dx.doi.org/10.1107/S2053230X16002715

[1]

[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='5b0n' size='340' side='right'caption='[[5b0n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5b0n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B0N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5b0n]] is a 2 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=5B0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B0N FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ipaH9.8, CP0226, pWR501_0234, SFLP090 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr>
+</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=5b0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0n OCA], [https://pdbe.org/5b0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b0n RCSB], [https://www.ebi.ac.uk/pdbsum/5b0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0n ProSAT]</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=5b0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0n OCA], [http://pdbe.org/5b0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b0n RCSB], [http://www.ebi.ac.uk/pdbsum/5b0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 ==See Also==
-*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
+*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Shigella paradysenteriae weldin 1927]]
 [[Category: Large Structures]]
-[[Category: Kim, M]]
+[[Category: Shigella flexneri]]
-[[Category: Mizushima, T]]
+[[Category: Kim M]]
-[[Category: Sasakawa, C]]
+[[Category: Mizushima T]]
-[[Category: Takagi, K]]
+[[Category: Sasakawa C]]
-[[Category: Effector]]
+[[Category: Takagi K]]
-[[Category: Ligase]]
-[[Category: Lrr domain]]
-[[Category: Ubiquitin ligase]]

5b0n: Difference between revisions

Revision as of 06:33, 31 May 2023

Structure of Shigella effector LRR domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools