PDBsum entry 3e46

Ligase

PDB id: 3e46

Contents

Protein chain

202 a.a.

Metals

_CA

Waters ×207

References listed in PDB file

Key reference

• Title: Structure of full-Length ubiquitin-Conjugating enzyme e2-25k (huntingtin-Interacting protein 2).
• Authors: R.C.Wilson, R.C.Hughes, J.W.Flatt, E.J.Meehan, J.D.Ng, P.D.Twigg.
• Ref.: Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009, 65, 440-444.
• PubMed id: 19407372

Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above have been manually determined.

Abstract

The ubiquitin-conjugating enzyme E2-25K has been identified as a huntingtin (the key protein in Huntington's disease) interacting protein and has been shown to play a role in mediating the toxicity of Abeta, the principal protein involved in Alzheimer's disease pathogenesis. E2-25K is a dual-domain protein with an ubiquitin-associated (UBA) domain as well as a conserved ubiquitin-conjugating (UBC) domain which catalyzes the formation of a covalent bond between the C-terminal glycine of an ubiquitin molecule and the -amine of a lysine residue on the acceptor protein as part of the ubiquitin-proteasome pathway. The crystal structures of E2-25K M172A mutant protein at pH 6.5 and pH 8.5 were determined to 1.9 and 2.2 A resolution, respectively. Examination of the structures revealed domain-domain interactions between the UBC and UBA domains which have not previously been reported.