Ubiquitin conjugating enzyme: Difference between revisions

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Michal Harel, Alexander Berchansky, David A Taves

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	<StructureSection load='~~1z2u~~' size='350' side='right' caption='Structure of ubiquitin conjugating enzyme 2 ~~comlex with butanediol and Cl- (green), Na+ (purple) ions~~ (PDB entry [[~~1z2u~~]])' scene=''>		<StructureSection load='1ayz' size='350' side='right' caption='Structure of human ubiquitin conjugating enzyme 2 (PDB entry [[1ayz]])' scene=''>

	'''Ubiquitin conjugating enzyme''' (Ubc) or '''E2 enzyme''' catalyzes the second step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (Ubc) cysteine. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. Ubc13 makes a catalytically active heterodimer with MMS2.		'''Ubiquitin conjugating enzyme''' (Ubc) or '''E2 enzyme''' catalyzes the second step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (Ubc) cysteine. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. Ubc13 makes a catalytically active heterodimer with MMS2.