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2lq7

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{{STRUCTURE_2lq7| PDB=2lq7 | SCENE= }}
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==E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition==
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===E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition===
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<StructureSection load='2lq7' size='340' side='right' caption='[[2lq7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_22821745}}
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Function==
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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>
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[[http://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>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[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].
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</div>
==See Also==
==See Also==
*[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]]
*[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:022821745</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Elgin, E S.]]
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[[Category: Elgin, E S]]
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[[Category: Peterson, F C.]]
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[[Category: Peterson, F C]]
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[[Category: Volkman, B F.]]
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[[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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