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== | ==Crystal structure of S. pombe Ubiquitin activating enzyme 1 (Uba1) in complex with ubiquitin and ATP/Mg== | ||
[[http://www.uniprot.org/uniprot/UBA1_SCHPO UBA1_SCHPO | <StructureSection load='4ii3' size='340' side='right'caption='[[4ii3]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ii3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4II3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4II3 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4ii3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ii3 OCA], [https://pdbe.org/4ii3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ii3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ii3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ii3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UBA1_SCHPO UBA1_SCHPO] 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 == | |||
Ubiquitin (Ub) conjugation is initiated by an E1 enzyme that catalyzes carboxy-terminal Ub adenylation, thioester bond formation to a catalytic cysteine in the E1 Cys domain, and thioester transfer to a catalytic cysteine in E2 conjugating enzymes. How the E1 and E2 active sites come together during thioester transfer and how Ub E1 interacts with diverse Ub E2s remains unclear. Here we present a crystal structure of a Ub E1-E2(Ubc4)/Ub/ATPMg complex that was stabilized by induction of a disulfide bond between the E1 and E2 active sites. The structure reveals combinatorial recognition of the E2 by the E1 ubiquitin-fold domain (UFD) and Cys domain and mutational analysis, coupled with thioester transfer assays with E1, Ubc4, and other Ub E2s, show that both interfaces are important for thioester transfer. Comparison to a Ub E1/Ub/ATPMg structure reveals conformational changes in the E1 that bring the E1 and E2 active sites together. | |||
Structure of a ubiquitin e1-e2 complex: insights to e1-e2 thioester transfer.,Olsen SK, Lima CD Mol Cell. 2013 Mar 7;49(5):884-96. doi: 10.1016/j.molcel.2013.01.013. Epub 2013, Feb 14. PMID:23416107<ref>PMID:23416107</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ii3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribosomal protein L40|Ribosomal protein L40]] | |||
*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Schizosaccharomyces pombe 972h-]] | [[Category: Schizosaccharomyces pombe 972h-]] | ||
[[Category: Lima CD]] | |||
[[Category: Lima | [[Category: Olsen SK]] | ||
[[Category: Olsen | |||
Latest revision as of 18:23, 20 September 2023
Crystal structure of S. pombe Ubiquitin activating enzyme 1 (Uba1) in complex with ubiquitin and ATP/MgCrystal structure of S. pombe Ubiquitin activating enzyme 1 (Uba1) in complex with ubiquitin and ATP/Mg
Structural highlights
FunctionUBA1_SCHPO 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. Publication Abstract from PubMedUbiquitin (Ub) conjugation is initiated by an E1 enzyme that catalyzes carboxy-terminal Ub adenylation, thioester bond formation to a catalytic cysteine in the E1 Cys domain, and thioester transfer to a catalytic cysteine in E2 conjugating enzymes. How the E1 and E2 active sites come together during thioester transfer and how Ub E1 interacts with diverse Ub E2s remains unclear. Here we present a crystal structure of a Ub E1-E2(Ubc4)/Ub/ATPMg complex that was stabilized by induction of a disulfide bond between the E1 and E2 active sites. The structure reveals combinatorial recognition of the E2 by the E1 ubiquitin-fold domain (UFD) and Cys domain and mutational analysis, coupled with thioester transfer assays with E1, Ubc4, and other Ub E2s, show that both interfaces are important for thioester transfer. Comparison to a Ub E1/Ub/ATPMg structure reveals conformational changes in the E1 that bring the E1 and E2 active sites together. Structure of a ubiquitin e1-e2 complex: insights to e1-e2 thioester transfer.,Olsen SK, Lima CD Mol Cell. 2013 Mar 7;49(5):884-96. doi: 10.1016/j.molcel.2013.01.013. Epub 2013, Feb 14. PMID:23416107[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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