Ubiquitin conjugating enzyme
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='3ptf' size='350' side='right' caption='Structure of human ubiquitin conjugating enzyme E2 (grey and green) complex with ubiquitin (yellow and pink) (PDB entry [[3ptf]])' 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 (E2) (Ubc) cysteine<ref>PMID:19549727</ref>. 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 /> | '''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 (E2) (Ubc) cysteine<ref>PMID:19549727</ref>. 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 /> | ||
Revision as of 11:19, 30 November 2016
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3D Structures of ubiquitin conjugating enzyme
Updated on 30-November-2016
References
- ↑ Markson G, Kiel C, Hyde R, Brown S, Charalabous P, Bremm A, Semple J, Woodsmith J, Duley S, Salehi-Ashtiani K, Vidal M, Komander D, Serrano L, Lehner P, Sanderson CM. Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network. Genome Res. 2009 Oct;19(10):1905-11. Epub 2009 Jun 23. PMID:19549727 doi:http://dx.doi.org/gr.093963.109
