4CCG

Structure of an E2-E3 complex

Summary for 4CCG

• Entry DOI: 10.2210/pdb4ccg/pdb
• Descriptor: UBIQUITIN-CONJUGATING ENZYME E2 T, E3 UBIQUITIN-PROTEIN LIGASE FANCL, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (10 entities in total)
• Functional Keywords: ligase
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: Q9NW38; Nucleus: Q9NPD8
• Total number of polymer chains: 4
• Total formula weight: 69553.08

Authors

Hodson, C.,Purkiss, A.,Walden, H. (deposition date: 2013-10-22, release date: 2014-01-08, Last modification date: 2023-12-20)

Primary citation

Hodson, C.,Purkiss, A.,Miles, J.A.,Walden, H.
Structure of the Human Fancl Ring-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection.
Structure, 22:337-, 2014

PubMed 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.

PubMed: 24389026
DOI: 10.1016/J.STR.2013.12.004

Experimental method

X-RAY DIFFRACTION (2.4 Å)