7r70
From Proteopedia
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==Crystal Structure of the UbArk2C fusion protein== | ==Crystal Structure of the UbArk2C fusion protein== | ||
| - | <StructureSection load='7r70' size='340' side='right'caption='[[7r70]]' scene=''> | + | <StructureSection load='7r70' size='340' side='right'caption='[[7r70]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R70 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7r70]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R70 FirstGlance]. <br> |
| - | </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=7r70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r70 OCA], [https://pdbe.org/7r70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r70 RCSB], [https://www.ebi.ac.uk/pdbsum/7r70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r70 ProSAT]</span></td></tr> | + | </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=ZN:ZINC+ION'>ZN</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></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=7r70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r70 OCA], [https://pdbe.org/7r70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r70 RCSB], [https://www.ebi.ac.uk/pdbsum/7r70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r70 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A large family of E3 ligases that contain both substrate recruitment and RING domains confer specificity within the ubiquitylation cascade. Regulation of RING E3s depends on modulating their ability to stabilise the RING bound E2~ubiquitin conjugate in the activated (or closed) conformation. Here we report the structure of the Ark2C RING bound to both a regulatory ubiquitin molecule and an activated E2~ubiquitin conjugate. The structure shows that the RING domain and non-covalently bound ubiquitin molecule together make contacts that stabilise the activated conformation of the conjugate, revealing why ubiquitin is a key regulator of Ark2C activity. We also identify a charged loop N-terminal to the RING domain that enhances activity by interacting with both the regulatory ubiquitin and ubiquitin conjugated to the E2. In addition, the structure suggests how Lys48-linked ubiquitin chains might be assembled by Ark2C and UbcH5b. Together this study identifies features common to RING E3s, as well elements that are unique to Ark2C and related E3s, which enhance assembly of ubiquitin chains. | ||
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| + | Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C.,Paluda A, Middleton AJ, Rossig C, Mace PD, Day CL Nat Commun. 2022 Mar 4;13(1):1181. doi: 10.1038/s41467-022-28782-y. PMID:35246518<ref>PMID:35246518</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7r70" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Day | + | [[Category: RING-type E3 ubiquitin transferase]] |
| - | [[Category: Mace | + | [[Category: Day, C L]] |
| - | [[Category: Middleton | + | [[Category: Mace, P D]] |
| - | [[Category: Paluda A]] | + | [[Category: Middleton, A J]] |
| + | [[Category: Paluda, A]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Ring e3 ligase ubiquitin ptm]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:39, 18 August 2022
Crystal Structure of the UbArk2C fusion protein
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