Ubiquitin conjugating enzyme

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Revision as of 07:30, 11 January 2016

Updated on 11-January-2016

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 <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.<br />
+For more details see [[UBC13 MMS2]].
 </StructureSection>