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.
Highlights
The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes
Further diversity arises from the existence of several ubiquitinlike protein modifiers, such as SUMO and NEDD8 that utilize their own enzymatic machineries and are associated with distinct physiological responses
This process begins by activation of the carboxyl terminus of ubiquitin by adenylation, followed by a thioesterification reaction in which ubiquitin is conjugated to a cysteine residue at the active site of the E1 enzyme
Summary
The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. The mechanism of HECT (homologous to the E6-AP C-terminus) domain-containing E3 enzymes includes an additional trans-thioesterification step, in which ubiquitin is linked to a catalytic cysteine on the E3.
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