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Open Access Review

Macromolecular juggling by ubiquitylation enzymes

Sonja Lorenz12, Aaron J Cantor12, Michael Rape12 and John Kuriyan12345*

Author Affiliations

1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA

2 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA

3 Department of Chemistry, University of California, Berkeley, CA 94720, USA

4 Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA

5 Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

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BMC Biology 2013, 11:65  doi:10.1186/1741-7007-11-65

Published: 25 June 2013

Abstract

The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. Members of the E1 and E3 enzyme families can undergo particularly large conformational changes during their catalytic cycles, involving the remodeling of domain interfaces. This enables the efficient, directed and regulated handover of ubiquitin from one carrier to the next one. We review some of these conformational transformations, as revealed by crystallographic studies.