Macromolecular Juggling by Ubiquitylation Enzymes

BMC Biol. 2013 Jun 25;11:65. doi: 10.1186/1741-7007-11-65.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biocatalysis
  • Humans
  • Macromolecular Substances / metabolism*
  • Phosphorylation
  • Protein Structure, Tertiary
  • Ubiquitin-Protein Ligase Complexes / chemistry
  • Ubiquitin-Protein Ligase Complexes / metabolism*
  • Ubiquitination*

Substances

  • Macromolecular Substances
  • Ubiquitin-Protein Ligase Complexes