Macromolecular juggling by ubiquitylation enzymes

BMC Biology

Review

Aaron J Cantor¹  Sonja Lorenz¹  Michael Rape¹  John Kuriyan² 

[1] Department of Molecular and Cell Biology, University of California, 94720, Berkeley, CA, USA;California Institute for Quantitative Biosciences, University of California, 94720, Berkeley, CA, USA;Department of Molecular and Cell Biology, University of California, 94720, Berkeley, CA, USA;California Institute for Quantitative Biosciences, University of California, 94720, Berkeley, CA, USA;Department of Chemistry, University of California, 94720, Berkeley, CA, USA;Howard Hughes Medical Institute, University of California, 94720, Berkeley, CA, USA;Physical Biosciences Division, Lawrence Berkeley National Laboratory, 94720, Berkeley, CA, USA;

关键词: Protein Data Bank;    Ring Domain;    Closed Conformation;    Ubiquitin Chain;    Catalytic Cysteine;   

DOI  :  10.1186/1741-7007-11-65

 received in 2012-11-01, accepted in 2013-06-18,  发布年份 2013

来源: Springer

【 摘 要 】

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.

【 授权许可】

Unknown   
© Lorenz et al; licensee BioMed Central Ltd. 2013. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.