3F92

Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting Protein 2) M172A mutant crystallized at pH 8.5

Summary for 3F92

• Entry DOI: 10.2210/pdb3f92/pdb
• Related: 1JBB 1YLA 3E46
• Descriptor: Ubiquitin-conjugating enzyme E2 K, TETRAETHYLENE GLYCOL, BETA-MERCAPTOETHANOL, ... (6 entities in total)
• Functional Keywords: ubiquitin-conjugating, huntington interacting, e2-25k, ligase, ubiquitin-conjugating enzyme e2 k, e2(25k), ubiquitin-protein ligase, ubiquitin carrier protein, huntington-interacting protein 2, hip-2, alternative splicing, cytoplasm, ubl conjugation, ubl conjugation pathway
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : P61086
• Total number of polymer chains: 1
• Total formula weight: 28834.65

Authors

Wilson, R.C.,Hughes, R.C.,Flatt, J.W.,Meehan, E.J.,Ng, J.D.,Twigg, P.D. (deposition date: 2008-11-13, release date: 2008-11-25, Last modification date: 2023-09-06)

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 (2.23 Å)