8fxf

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the coiled-coil domain of TRIM56

Structural highlights

8fxf is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRI56_MOUSE E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1 (PubMed:21074459, PubMed:29426904). In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta (PubMed:21074459). Also mediates monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation (PubMed:29426904). Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling (By similarity). Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (By similarity).[UniProtKB:Q9BRZ2]^[1] ^[2]

Publication Abstract from PubMed

Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to facilitate direct ubiquitin transfer. However, the quaternary structures of RING E3 ligases that perform ubiquitin transfer remain poorly understood. In this study, we solved the crystal structure of TRIM56, a member of the RING E3 ligase. The structure of the coiled-coil domain indicated that the two anti-parallel dimers bound together to form a tetramer at a small crossing angle. This tetramer structure allows two RING domains to exist on each side to form an active homodimer in supporting ubiquitin transfer from E2 to its nearby substrate recruited by the C-terminal domains on the same side. These findings suggest that the coiled-coil domain-mediated tetramer is a feasible scaffold for facilitating the recruitment and transfer of ubiquitin to accomplish E3 ligase activity.

TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.,Lou X, Ma B, Zhuang Y, Xiao X, Minze LJ, Xing J, Zhang Z, Li XC Comput Struct Biotechnol J. 2023 Apr 23;21:2801-2808. doi: , 10.1016/j.csbj.2023.04.022. eCollection 2023. PMID:37168870^[3]

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

References

↑ Tsuchida T, Zou J, Saitoh T, Kumar H, Abe T, Matsuura Y, Kawai T, Akira S. The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA. Immunity. 2010 Nov 24;33(5):765-76. doi: 10.1016/j.immuni.2010.10.013. Epub 2010 , Nov 11. PMID:21074459 doi:10.1016/j.immuni.2010.10.013
↑ Seo GJ, Kim C, Shin WJ, Sklan EH, Eoh H, Jung JU. TRIM56-mediated monoubiquitination of cGAS for cytosolic DNA sensing. Nat Commun. 2018 Feb 9;9(1):613. PMID:29426904 doi:10.1038/s41467-018-02936-3
↑ Lou X, Ma B, Zhuang Y, Xiao X, Minze LJ, Xing J, Zhang Z, Li XC. TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions. Comput Struct Biotechnol J. 2023 Apr 23;21:2801-2808. PMID:37168870 doi:10.1016/j.csbj.2023.04.022

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/8fxf"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8fxf is ON HOLD  until Paper Publication
+==Crystal structure of the coiled-coil domain of TRIM56==
+<StructureSection load='8fxf' size='340' side='right'caption='[[8fxf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8fxf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FXF 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=8fxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fxf OCA], [https://pdbe.org/8fxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fxf RCSB], [https://www.ebi.ac.uk/pdbsum/8fxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fxf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRI56_MOUSE TRI56_MOUSE] E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1 (PubMed:21074459, PubMed:29426904). In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta (PubMed:21074459). Also mediates monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation (PubMed:29426904). Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling (By similarity). Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (By similarity).[UniProtKB:Q9BRZ2]<ref>PMID:21074459</ref> <ref>PMID:29426904</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to facilitate direct ubiquitin transfer. However, the quaternary structures of RING E3 ligases that perform ubiquitin transfer remain poorly understood. In this study, we solved the crystal structure of TRIM56, a member of the RING E3 ligase. The structure of the coiled-coil domain indicated that the two anti-parallel dimers bound together to form a tetramer at a small crossing angle. This tetramer structure allows two RING domains to exist on each side to form an active homodimer in supporting ubiquitin transfer from E2 to its nearby substrate recruited by the C-terminal domains on the same side. These findings suggest that the coiled-coil domain-mediated tetramer is a feasible scaffold for facilitating the recruitment and transfer of ubiquitin to accomplish E3 ligase activity.
-Authors:
+TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.,Lou X, Ma B, Zhuang Y, Xiao X, Minze LJ, Xing J, Zhang Z, Li XC Comput Struct Biotechnol J. 2023 Apr 23;21:2801-2808. doi: , 10.1016/j.csbj.2023.04.022. eCollection 2023. PMID:37168870<ref>PMID:37168870</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 8fxf" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Li XC]]
+[[Category: Lou XH]]
+[[Category: Ma BB]]
+[[Category: Zhuang Y]]

8fxf

From Proteopedia

Current revision

Crystal structure of the coiled-coil domain of TRIM56

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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