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7w0s

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TRIM7 in complex with C-terminal peptide of 2C

Structural highlights

7w0s is a 6 chain structure with sequence from Coxsackievirus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.4Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRIM7_HUMAN E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (PubMed:25851810). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of proinflammatory cytokines and type I interferon (By similarity). Plays also a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation (PubMed:32126128).[UniProtKB:Q923T7]^[1] ^[2] (Microbial infection) Promotes Zika virus replication by mediating envelope protein E ubiquitination.^[3]

Publication Abstract from PubMed

The E3 ligase TRIM7 has emerged as a critical player in viral infection and pathogenesis. However, the mechanism governing the TRIM7-substrate association remains to be defined. Here we report the crystal structures of TRIM7 in complex with 2C peptides of human enterovirus. Structure-guided studies reveal the C-terminal glutamine residue of 2C as the primary determinant for TRIM7 binding. Leveraged by this finding, we identify norovirus and SARS-CoV-2 proteins, and physiological proteins, as new TRIM7 substrates. Crystal structures of TRIM7 in complex with multiple peptides derived from SARS-CoV-2 proteins display the same glutamine-end recognition mode. Furthermore, TRIM7 could trigger the ubiquitination and degradation of these substrates, possibly representing a new Gln/C-degron pathway. Together, these findings unveil a common recognition mode by TRIM7, providing the foundation for further mechanistic characterization of antiviral and cellular functions of TRIM7.

A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7 structures.,Liang X, Xiao J, Li X, Liu Y, Lu Y, Wen Y, Li Z, Che X, Ma Y, Zhang X, Zhang Y, Jian D, Wang P, Xuan C, Yu G, Li L, Zhang H Nat Chem Biol. 2022 Aug 18. pii: 10.1038/s41589-022-01128-x. doi:, 10.1038/s41589-022-01128-x. PMID:35982226^[4]

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

References

↑ Chakraborty A, Diefenbacher ME, Mylona A, Kassel O, Behrens A. The E3 ubiquitin ligase Trim7 mediates c-Jun/AP-1 activation by Ras signalling. Nat Commun. 2015 Apr 8;6:6782. doi: 10.1038/ncomms7782. PMID:25851810 doi:http://dx.doi.org/10.1038/ncomms7782
↑ Yang B, Liu Y, Cui Y, Song D, Zhang G, Ma S, Liu Y, Chen M, Chen F, Wang H, Wang J. RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation. PLoS Pathog. 2020 Mar 3;16(3):e1008387. doi: 10.1371/journal.ppat.1008387., eCollection 2020 Mar. PMID:32126128 doi:http://dx.doi.org/10.1371/journal.ppat.1008387
↑ Giraldo MI, Xia H, Aguilera-Aguirre L, Hage A, van Tol S, Shan C, Xie X, Sturdevant GL, Robertson SJ, McNally KL, Meade-White K, Azar SR, Rossi SL, Maury W, Woodson M, Ramage H, Johnson JR, Krogan NJ, Morais MC, Best SM, Shi PY, Rajsbaum R. Envelope protein ubiquitination drives entry and pathogenesis of Zika virus. Nature. 2020 Sep;585(7825):414-419. doi: 10.1038/s41586-020-2457-8. Epub 2020 Jul, 8. PMID:32641828 doi:http://dx.doi.org/10.1038/s41586-020-2457-8
↑ Liang X, Xiao J, Li X, Liu Y, Lu Y, Wen Y, Li Z, Che X, Ma Y, Zhang X, Zhang Y, Jian D, Wang P, Xuan C, Yu G, Li L, Zhang H. A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7 structures. Nat Chem Biol. 2022 Aug 18. pii: 10.1038/s41589-022-01128-x. doi:, 10.1038/s41589-022-01128-x. PMID:35982226 doi:http://dx.doi.org/10.1038/s41589-022-01128-x

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/7w0s"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7w0s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxsackievirus Coxsackievirus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W0S FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w0s OCA], [https://pdbe.org/7w0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w0s RCSB], [https://www.ebi.ac.uk/pdbsum/7w0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w0s ProSAT]</span></td></tr>
 </table>

7w0s

From Proteopedia

Current revision

TRIM7 in complex with C-terminal peptide of 2C

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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