7zh9
From Proteopedia
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==Uba1 in complex with ATP== | ==Uba1 in complex with ATP== | ||
| - | <StructureSection load='7zh9' size='340' side='right'caption='[[7zh9]]' scene=''> | + | <StructureSection load='7zh9' size='340' side='right'caption='[[7zh9]], [[Resolution|resolution]] 1.72Å' 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=7ZH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZH9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7zh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZH9 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=7zh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zh9 OCA], [https://pdbe.org/7zh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zh9 RCSB], [https://www.ebi.ac.uk/pdbsum/7zh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zh9 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7zh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zh9 OCA], [https://pdbe.org/7zh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zh9 RCSB], [https://www.ebi.ac.uk/pdbsum/7zh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zh9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/UBA1_YEAST UBA1_YEAST]] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The covalent modification of target proteins with ubiquitin or ubiquitin-like modifiers is initiated by E1 activating enzymes, which typically transfer a single modifier onto cognate conjugating enzymes. UBA6 is an unusual E1 since it activates two highly distinct modifiers, ubiquitin and FAT10. Here, we report crystal structures of UBA6 in complex with either ATP or FAT10. In the UBA6-FAT10 complex, the C-terminal domain of FAT10 binds to where ubiquitin resides in the UBA1-ubiquitin complex, however, a switch element ensures the alternate recruitment of either modifier. Simultaneously, the N-terminal domain of FAT10 interacts with the 3-helix bundle of UBA6. Site-directed mutagenesis identifies residues permitting the selective activation of either ubiquitin or FAT10. These results pave the way for studies investigating the activation of either modifier by UBA6 in physiological and pathophysiological settings. | ||
| + | |||
| + | Structures of UBA6 explain its dual specificity for ubiquitin and FAT10.,Truongvan N, Li S, Misra M, Kuhn M, Schindelin H Nat Commun. 2022 Aug 15;13(1):4789. doi: 10.1038/s41467-022-32040-6. PMID:35970836<ref>PMID:35970836</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7zh9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Misra M]] | [[Category: Misra M]] | ||
[[Category: Schindelin H]] | [[Category: Schindelin H]] | ||
Revision as of 19:35, 7 September 2022
Uba1 in complex with ATP
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