1Y8R

SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1-MG-ATP COMPLEX

Summary for 1Y8R

• Entry DOI: 10.2210/pdb1y8r/pdb
• Related: 1Y8Q
• Descriptor: Ubiquitin-like 1 activating enzyme E1A, Ubiquitin-like 2 activating enzyme E1B, Ubiquitin-like protein SMT3C, ... (7 entities in total)
• Functional Keywords: sumo; e1; heterodimer; activating enzyme; ubl, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9UBE0 Q9UBT2; Nucleus membrane: P63165
• Total number of polymer chains: 6
• Total formula weight: 243057.35

Authors

Lois, L.M.,Lima, C.D. (deposition date: 2004-12-13, release date: 2005-01-25, Last modification date: 2024-02-14)

Primary citation

Lois, L.M.,Lima, C.D.
Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
Embo J., 24:439-451, 2005

PubMed 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 A 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 A 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.

PubMed: 15660128
DOI: 10.1038/sj.emboj.7600552

Experimental method

X-RAY DIFFRACTION (2.75 Å)