And yet it moves: active site remodeling in the SUMO E1

Daniel Völler; Hermann Schindelin

doi:10.1016/j.str.2010.03.005

And yet it moves: active site remodeling in the SUMO E1

Structure. 2010 Mar 14;18(4):419-21. doi: 10.1016/j.str.2010.03.005.

Authors

Daniel Völler¹, Hermann Schindelin

Affiliation

¹ Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Josef-Schneider-Str. 2, 97080 Würzburg, Germany.

PMID: 20399179
DOI: 10.1016/j.str.2010.03.005

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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