Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1 Journal Article
| Authors: | Lois, L. M.; Lima, C. D. |
| Article Title: | Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1 |
| Abstract: | E1 enzymes facilitate conjugation of ubiquitin and ubiquitin-like proteins through adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating proteins. Structures of human heterodimeric Sae1/Sae2-Mg · ATP and Sae1/Sae2-SUMO-1-Mg · ATP complexes were determined at 2.2 and 2.75 Å resolution, respectively. Despite the presence of Mg · ATP, the Sae1/Sae2-SUMO-1-Mg · ATP structure reveals a substrate complex insomuch as the SUMO C-terminus remains unmodified within the adenylation site and 35 Å from the catalytic cysteine, suggesting that additional changes within the adenylation site may be required to facilitate chemistry prior to adenylation and thioester transfer. A mechanism for E2 recruitment to E1 is suggested by biochemical and genetic data, each of which supports a direct role for the E1 C-terminal ubiquitin-like domain for E2 recruitment during conjugation. © 2005 European Molecular Biology Organization. |
| Keywords: | unclassified drug; nonhuman; ubiquitin; polymerase chain reaction; protein domain; complex formation; ubiquitin protein ligase; carboxy terminal sequence; enzyme activation; amino acid sequence; molecular sequence data; sequence homology, amino acid; recombinant proteins; models, molecular; dimerization; crystallography, x-ray; protein structure, tertiary; multiprotein complexes; conformational transition; catalysis; adenosine triphosphate; protein structure; point mutation; sumo-1 protein; ubiquitin-activating enzymes; catalytic domain; cysteine; thioester; ubiquitins; ubiquitin conjugating enzyme; adenylation; x ray diffraction; conjugation; sumo 1 protein; protein sae2; aos1; sae1; sae2; uba2; adenosine triphosphate magnesium; protein sae1 |
| Journal Title: | EMBO Journal |
| Volume: | 24 |
| Issue: | 3 |
| ISSN: | 0261-4189 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2005-02-09 |
| Start Page: | 439 |
| End Page: | 451 |
| Language: | English |
| DOI: | 10.1038/sj.emboj.7600552 |
| PUBMED: | 15660128 |
| PROVIDER: | scopus |
| PMCID: | PMC548657 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 102" - "Export Date: 24 October 2012" - "CODEN: EMJOD" - "Source: Scopus" |
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