Article
- The EMBO Journal (2005) 24, 439 - 451
- doi:10.1038/sj.emboj.7600552
Published online: 20 January 2005
Subject Categories:
Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
Luisa Maria Lois1,a and Christopher D Lima1
- Structural Biology Program, Sloan-Kettering Institute, New York, NY, USA
Correspondence to:
Christopher D Lima, Structural Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA. Tel.: +1 212 639 8205; Fax: +1 212 717 3047; E-mail: limac@mskcc.org
aPresent address: Dept de Bioquímica I Biologia Molecular, Universitat de Barcelona, c/ Martí i Franquès, 1, Barcelona 08028, Spain
Received 20 October 2004; Accepted 21 December 2004
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-MgATP complexes were determined at 2.2 and 2.75 Å resolution, respectively. Despite the presence of MgATP, the Sae1/Sae2-SUMO-1-MgATP 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.
Keywords:
- Aos1,
- conjugation,
- Sae1,
- Sae2,
- Uba2
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