3kyc
Human SUMO E1 complex with a SUMO1-AMP mimicHuman SUMO E1 complex with a SUMO1-AMP mimic
E1 enzymes activate ubiquitin (Ub) and ubiquitin-like (Ubl) proteins in two steps by carboxy-terminal adenylation and thioester bond formation to a conserved catalytic cysteine in the E1 Cys domain. The structural basis for these intermediates remains unknown. Here we report crystal structures for human SUMO E1 in complex with SUMO adenylate and tetrahedral intermediate analogues at 2.45 and 2.6 A, respectively. These structures show that side chain contacts to ATP.Mg are released after adenylation to facilitate a 130 degree rotation of the Cys domain during thioester bond formation that is accompanied by remodelling of key structural elements including the helix that contains the E1 catalytic cysteine, the crossover and re-entry loops, and refolding of two helices that are required for adenylation. These changes displace side chains required for adenylation with side chains required for thioester bond formation. Mutational and biochemical analyses indicate these mechanisms are conserved in other E1s.
Active site remodelling accompanies thioester bond formation in the SUMO E1., Olsen SK, Capili AD, Lu X, Tan DS, Lima CD, Nature. 2010 Feb 18;463(7283):906-12. PMID:20164921
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this StructureAbout this Structure
3kyc is a 3 chain structure of Human SUMO E1 complex and SUMO with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
- Human SUMO E1 complex
- Human SUMO E1 complex with a SUMO1-AMP mimic
- Human SUMO E1~SUMO1-AMP tetrahedral intermediate mimic
- SUMO
ReferenceReference
- ↑ Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 2010 Feb 18;463(7283):906-12. PMID:20164921 doi:10.1038/nature08765