Structure of the human FANCL RING-Ube2T complex reveals determinants of cognate E3-E2 selection

Hodson, C., Purkiss, A., Miles, J. A. and Walden, H. (2014) Structure of the human FANCL RING-Ube2T complex reveals determinants of cognate E3-E2 selection. Structure, 22(2), pp. 337-344. (doi: 10.1016/j.str.2013.12.004) (PMID:24389026) (PMCID:PMC3979106)

Abstract

The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic E3-E2 interactions are well established. Nevertheless, the determinants of selective, specific E3-E2 recognition are not understood. There are ∼40 E2s and ∼600 E3s giving rise to a possible ∼24,000 E3-E2 pairs. Using the Fanconi Anemia pathway exclusive E3-E2 pair, FANCL-Ube2T, we report the atomic structure of the FANCL RING-Ube2T complex, revealing a specific and extensive network of additional electrostatic and hydrophobic interactions. Furthermore, we show that these specific interactions are required for selection of Ube2T over other E2s by FANCL.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Walden, Professor Helen
• Authors: Hodson, C., Purkiss, A., Miles, J. A., and Walden, H.
• College/School: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
• Journal Name: Structure
• Publisher: Elsevier (Cell Press)
• ISSN: 0969-2126
• ISSN (Online): 1878-4186
• Published Online: 02 January 2014
• Copyright Holders: Copyright © 2014 The Authors
• First Published: First published in Structure 22(2):337-344
• Publisher Policy: Reproduced under a Creative Commons License