Macromolecular juggling by ubiquitylation enzymes
| Autor: | Michael Rape, Aaron J. Cantor, John Kuriyan, Sonja Lorenz |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Physiology
Macromolecular Substances Plant Science Review Ubiquitin-conjugating enzyme General Biochemistry Genetics and Molecular Biology Protein structure Ubiquitin Structural Biology Animals Humans Phosphorylation Ecology Evolution Behavior and Systematics chemistry.chemical_classification biology Agricultural and Biological Sciences(all) Biochemistry Genetics and Molecular Biology(all) Ubiquitination Ubiquitin-Protein Ligase Complexes Cell Biology Ubiquitin ligase Cell biology Protein Structure Tertiary Enzyme chemistry biology.protein Biocatalysis General Agricultural and Biological Sciences Developmental Biology Biotechnology Macromolecule |
| Zdroj: | BMC Biology Lorenz, Sonja; Cantor, Aaron J; Rape, Michael; & Kuriyan, John. (2013). Macromolecular juggling by ubiquitylation enzymes. BMC Biology, 11(1), 65. doi: http://dx.doi.org/10.1186/1741-7007-11-65. Retrieved from: http://www.escholarship.org/uc/item/5dm6t06f |
| ISSN: | 1741-7007 |
| DOI: | 10.1186/1741-7007-11-65. |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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