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1y8q

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1y8q, resolution 2.25Å ()
Ligands: , ,
Gene: UBLE1A, SAE1 (Homo sapiens), UBLE1B, SAE2 (Homo sapiens)
Domains: Aos1_SUMO, Ube1_repeat1, Uba2_SUMO
Related: 1y8r
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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.

Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1., Lois LM, Lima CD, EMBO J. 2005 Feb 9;24(3):439-51. Epub 2005 Jan 20. PMID:15660128

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1Y8Q is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Lois LM, Lima CD. Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. EMBO J. 2005 Feb 9;24(3):439-51. Epub 2005 Jan 20. PMID:15660128

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