2lq7
From Proteopedia
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| - | + | ==E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition== | |
| - | + | <StructureSection load='2lq7' size='340' side='right' caption='[[2lq7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2lq7]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LQ7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBA3, UBE1C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lq7 RCSB], [http://www.ebi.ac.uk/pdbsum/2lq7 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
==See Also== | ==See Also== | ||
*[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]] | *[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Elgin, E S | + | [[Category: Elgin, E S]] |
| - | [[Category: Peterson, F C | + | [[Category: Peterson, F C]] |
| - | [[Category: Volkman, B F | + | [[Category: Volkman, B F]] |
[[Category: Beta grasp domain]] | [[Category: Beta grasp domain]] | ||
[[Category: E1 enzyme]] | [[Category: E1 enzyme]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 12:28, 18 December 2014
E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition
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