3E46

Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting protein 2) M172A mutant

Summary for 3E46

• Entry DOI: 10.2210/pdb3e46/pdb
• Related: 1JBB 1YLA 2BEP 2BF9
• Descriptor: Ubiquitin-conjugating enzyme E2-25 kDa, CALCIUM ION (3 entities in total)
• Functional Keywords: ubiquitin-conjugating, huntington interacting, e2-25k, ligase, alternative splicing, cytoplasm, ubl conjugation, ubl conjugation pathway
• Biological source: Homo sapiens
• Cellular location: Cytoplasm (By similarity): P61086
• Total number of polymer chains: 1
• Total formula weight: 28245.92

Authors

Hughes, R.C.,Wilson, R.C.,Flatt, J.W.,Meehan, E.J.,Ng, J.D.,Twigg, P.D. (deposition date: 2008-08-09, release date: 2008-08-26, Last modification date: 2023-08-30)

Primary citation

Wilson, R.C.,Hughes, R.C.,Flatt, J.W.,Meehan, E.J.,Ng, J.D.,Twigg, P.D.
Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
Acta Crystallogr.,Sect.F, 65:440-444, 2009

PubMed 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.

PubMed: 19407372
DOI: 10.1107/S1744309109011117

Experimental method

X-RAY DIFFRACTION (1.86 Å)