7bbf: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 7bbf~~ is ~~ON HOLD until sometime~~ in the ~~future~~

==Crystal structure of ubiquitin charged Ube2N (Ube2N~Ub) in complex with Ube2V2==

== Structural highlights ==

<table><tr><td colspan='2'>[[7bbf]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BBF 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]] 2.54Å</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=7bbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bbf OCA], [https://pdbe.org/7bbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bbf RCSB], [https://www.ebi.ac.uk/pdbsum/7bbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bbf ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/UB2V2_HUMAN UB2V2_HUMAN] Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.<ref>PMID:9705497</ref> <ref>PMID:10089880</ref> <ref>PMID:14562038</ref> <ref>PMID:20061386</ref>

== Publication Abstract from PubMed ==

Attachment of ubiquitin (Ub) to proteins is one of the most abundant and versatile of all posttranslational modifications and affects outcomes in essentially all physiological processes. RING E3 ligases target E2 Ub-conjugating enzymes to the substrate, resulting in its ubiquitination. However, the mechanism by which a ubiquitin chain is formed on the substrate remains elusive. Here we demonstrate how substrate binding can induce a specific RING topology that enables self-ubiquitination. By analyzing a catalytically trapped structure showing the initiation of TRIM21 RING-anchored ubiquitin chain elongation, and in combination with a kinetic study, we illuminate the chemical mechanism of ubiquitin conjugation. Moreover, biochemical and cellular experiments show that the topology found in the structure can be induced by substrate binding. Our results provide insights into ubiquitin chain formation on a structural, biochemical and cellular level with broad implications for targeted protein degradation.

~~Authors~~:

RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination.,Kiss L, Clift D, Renner N, Neuhaus D, James LC Nat Commun. 2021 Feb 22;12(1):1220. doi: 10.1038/s41467-021-21443-6. PMID:33619271<ref>PMID:33619271</ref>

~~Description~~:

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

[[Category: ~~Unreleased~~ Structures]]

</div>

==See Also==

*[[3D structures of ubiquitin|3D structures of ubiquitin]]

*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: James LC]]

[[Category: Kiss L]]

[[Category: Neuhaus D]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7bbf is ON HOLD  until sometime in the future
+==Crystal structure of ubiquitin charged Ube2N (Ube2N~Ub) in complex with Ube2V2==
+<StructureSection load='7bbf' size='340' side='right'caption='[[7bbf]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7bbf]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BBF 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]] 2.54&#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=7bbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bbf OCA], [https://pdbe.org/7bbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bbf RCSB], [https://www.ebi.ac.uk/pdbsum/7bbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bbf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/UB2V2_HUMAN UB2V2_HUMAN] Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.<ref>PMID:9705497</ref> <ref>PMID:10089880</ref> <ref>PMID:14562038</ref> <ref>PMID:20061386</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Attachment of ubiquitin (Ub) to proteins is one of the most abundant and versatile of all posttranslational modifications and affects outcomes in essentially all physiological processes. RING E3 ligases target E2 Ub-conjugating enzymes to the substrate, resulting in its ubiquitination. However, the mechanism by which a ubiquitin chain is formed on the substrate remains elusive. Here we demonstrate how substrate binding can induce a specific RING topology that enables self-ubiquitination. By analyzing a catalytically trapped structure showing the initiation of TRIM21 RING-anchored ubiquitin chain elongation, and in combination with a kinetic study, we illuminate the chemical mechanism of ubiquitin conjugation. Moreover, biochemical and cellular experiments show that the topology found in the structure can be induced by substrate binding. Our results provide insights into ubiquitin chain formation on a structural, biochemical and cellular level with broad implications for targeted protein degradation.
-Authors:
+RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination.,Kiss L, Clift D, Renner N, Neuhaus D, James LC Nat Commun. 2021 Feb 22;12(1):1220. doi: 10.1038/s41467-021-21443-6. PMID:33619271<ref>PMID:33619271</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 7bbf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
+*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: James LC]]
+[[Category: Kiss L]]
+[[Category: Neuhaus D]]