Abstract
The activation of ubiquitin and ubiquin-like proteins is catalyzed by E1 enzymes via consecutive adenylation and thioesterification reactions involving two apparently distant active sites. Olsen et al. (2010) uncover dramatic conformational changes in the SUMO E1 that spatially merge the adenylation and thioesterification active sites, including a > 30 A movement of the active site cysteine.
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