2lq7
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2lq7 is ON HOLD until Paper Publication Authors: Elgin, E.S., Peterson, F.C., Volkman, B.F. Description: E2 binding surface on Uba3 beta-grasp doma...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition== | |
| + | <StructureSection load='2lq7' size='340' side='right'caption='[[2lq7]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lq7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQ7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq7 OCA], [https://pdbe.org/2lq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lq7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UBA3_HUMAN UBA3_HUMAN] Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.<ref>PMID:10207026</ref> <ref>PMID:9694792</ref> <ref>PMID:12740388</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The covalent attachment of ubiquitin (Ub) and ubiquitin-like (Ubl) proteins to various eukaryotic targets plays critical roles in regulating numerous cellular processes. E1-activating enzymes are critical, because they catalyze activation of their cognate Ub/Ubl protein and are responsible for its transfer to the correct E2-conjugating enzyme(s). The activating enzyme for neural-precursor-cell-expressed developmentally downregulated 8 (NEDD8) is a heterodimer composed of APPBP1 and Uba3 subunits. The carboxyl terminal ubiquitin-like beta-grasp domain of human Uba3 (Uba3-betaGD) has been suggested as a key E2-binding site defining E2 specificity. In crystal structures of free E1 and the NEDD8-E1 complex, the E2-binding surface on the domain was missing from the electron density. However, when complexed with various E2s, this missing segment adopts a kinked alpha-helix. Here, we demonstrate that Uba3-betaGD is an independently folded domain in solution and that residues involved in E2 binding are absent from the NMR spectrum, indicating that the E2-binding surface on Uba3-betaGD interconverts between multiple conformations, analogous to a similar conformational transition observed in the E2-binding surface of SUMO E1. These results suggest that access to multiple conformational substates is an important feature of the E1-E2 interaction. | ||
| - | + | E2-binding surface on Uba3 beta-grasp domain undergoes a conformational transition.,Elgin ES, Sokmen N, Peterson FC, Volkman BF, Dag C, Haas AL Proteins. 2012 Oct;80(10):2482-7. doi: 10.1002/prot.24148. Epub 2012 Jul 31. PMID:22821745<ref>PMID:22821745</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2lq7" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Elgin ES]] | ||
| + | [[Category: Peterson FC]] | ||
| + | [[Category: Volkman BF]] | ||
Current revision
E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition
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